中文   |   English   |   Email Alert
Fig/Tab
Advanced Search
image

Recent Advances in Peptide-Based Electrochemical Biosensor

Han Zhang , Jiawang Ding , Wei Qin

Progress in Chemistry ›› 2021, Vol. 33 ›› Issue (10) : 1756 -1765.

PDF
Progress in Chemistry ›› 2021, Vol. 33 ›› Issue (10) : 1756-1765 DOI: 10.7536/PC200855
research-article
Scan to read & Share
Recent Advances in Peptide-Based Electrochemical Biosensor
Author information +
History +
PDF

Abstract

Peptides with unique features such as small molecular weight, ease synthesis, good biocompatibility, high stability and versatile sequences, have received increasing interest as recognition elements for biosensors. Electrochemical analysis has wide applications because of its high sensitivity, good accuracy, simple equipment, wide detection range and easy to use. The peptide-based electrochemical biosensors can be used in many fields including environment monitoring, biomedicine and food detection. In this review, we introduce the peptide-based electrochemical biosensors for detection heavy metal ions, small-molecules, proteins, pathogenic bacteria and viruses. The strategies for peptide modification and immobilization are summarized. We also describe the properties and sensing mechanisms of peptide-based electrochemical biosensors. Sensing strategies especially those based on target-binding induced combination, digestion and phosphorylation of peptides have been discussed. Lastly, the current problems and prospect of the research on peptide-based electrochemical biosensor are discussed and prospected.

Contents

1 Introduction

2 Overview of peptide

3 Peptide-based electrochemical biosensor

3.1 Identification and detection of heavy metal ions

3.2 Identification and detection of small molecules

3.3 Identification and detection of proteins

3.4 Identification and detection of bacteria and viruses

4 Conclusions and prospects

Graphical abstract

Keywords

peptide / biosensor / electrochemical analysis / recognition molecule / detection

Cite this article

Download citation ▾
Han Zhang, Jiawang Ding, Wei Qin. Recent Advances in Peptide-Based Electrochemical Biosensor. Progress in Chemistry, 2021, 33(10): 1756-1765 DOI:10.7536/PC200855

登录浏览全文

4963

注册一个新账户 忘记密码

1 Introduction

With the help of sensory organs, people get information from nature and recognize nature. Nature imparts inspiration to human beings, and human beings learn from nature. Sensors are the senses or devices developed by human beings in the process of understanding nature and themselves. The core components of the sensor include an identification sensitive element and a signal conducting element. Inspired by nature, people use biological materials as sensitive elements of sensors, develop biosensors, and widely use biosensing technology in medical diagnosis, environmental monitoring, industrial production, food safety and many other fields.
To date, researchers have developed a variety of biosensors. According to their recognition sensitive elements, they are mainly divided into the following six categories: enzyme sensors, nucleic acid sensors, immunosensors, tissue sensors, microbial sensors and cell sensors. With the emergence of new materials, the development of new technologies and the expansion of applications, the construction of new biosensors based on new molecular recognition elements is attracting more and more attention. In recent years, the discovery and development of new recognition elements, such as artificial mimetic enzymes, molecularly imprinted polymers, deoxyribozymes, peptide nucleases, nucleic acid aptamers and polypeptides, are gradually promoting the new development of biosensing technology. In addition, the emergence of new biosensing mechanisms and the development of computer pattern recognition technology have greatly expanded the application space of biosensing.
Peptide is a ubiquitous biological macromolecule in nature, which plays a vital role in many life activities. In recent years, polypeptide-based biosensing technology, biomaterials and biomedicine have attracted much attention[1]. Researchers have developed peptide sensors based on optical (e.g., fluorescence, colorimetric analysis), electrochemical, and mass transfer[2,3]. The electrochemical sensor is a device that converts the chemical quantity of an object to be detected into an electrical quantity for detection based on the electrochemical properties of the object to be detected. It has the advantages of simplicity, portability, low cost, high sensitivity and continuous and rapid detection, and is an ideal signal conduction element. In this paper, the application of peptides as novel recognition molecules in electrochemical sensing analysis in the past five years is reviewed, in order to explore the new research and analytical applications of peptide-based biosensing technology.

2 Overview of Peptides

Peptides are polymers formed by the dehydration condensation of two or more amino acids. Polypeptides and proteins are usually distinguished by the number of amino acids (molecular weight). Polypeptides are a class of compounds that are intermediate between amino acids and proteins, usually with a molecular weight of less than 1000 Da, and are permeable to semipermeable membranes. Polypeptides can be divided into bioactive peptides and synthetic peptides. In 1963, Robert Bruce Merrifield founded the solid-phase synthesis of peptides, and won the Nobel Prize in Chemistry for his breakthrough in the field of peptide synthesis. In the 1980s, scientists established phage display technology to fuse exogenous peptide or protein genes with phage specific protein genes on its surface. This new biological technique has been successfully applied to polypeptide display and can obtain polypeptides with high specific recognition of targets in random libraries[4]. In a word, both solid phase peptide synthesis and phage display technology can produce a large number of highly purified polypeptides at low cost and quickly. The rapid synthesis and functionalization of peptides promote their wide applications in the fields of biosensing, drug development and delivery, and the synthesis of new materials.

3 Application of Peptide Electrochemical Biosensor

Compared with traditional biological macromolecules, peptides have the advantages of small molecular weight, easy modification, easy synthesis, low price, use under extreme conditions, good biological compatibility and non-toxic side effects, which are potential biological recognition elements[5]. Polypeptides have better biological stability than antibodies or DNA recognition elements including functionalized aptamers[6]. Polypeptides are composed of 20 amino acids, so there are more possibilities for combinations in sequence and length. In addition, the differences in hydrophilicity/hydrophobicity and charge of different amino acids are also conducive to the synthesis of polypeptides with diverse properties. Based on peptide self-assembly, researchers can also construct nanostructures with a variety of morphologies[7].
The immobilization of peptides on the electrode surface is very important for the construction of peptide-based electrochemical biosensors, which mainly includes electrostatic binding and covalent bonding. Researchers usually immobilize positively or negatively charged polypeptides on the surface of electrodes modified by specific materials through electrostatic interaction. In addition, researchers have developed a variety of covalent immobilization methods, including: (1) self-assembly based on Au — S bond, using cysteine at one end of polypeptide to self-assemble on the surface of gold electrode or gold nanoparticle modified electrode through Au — S bond (Fig. 1A); (2) covalent coupling based on amino group or carboxyl group,An amino group or a carboxyl group at one end of the polypeptide is grafted onto the surface of the functionalized electrode material by using a coupling agent or the amino group is covalently bonded by using glutaraldehyde as a cross-linking agent (fig. 1A, B); (3) phage-based immobilization,Peptides displayed on the surface of phage were modified on the electrode surface by phage (fig. 1C); (4) Based on biotin-avidin interaction, biotin-modified peptides and streptavidin-modified magnetic beads produced affinity (fig. 1D).
The polypeptide electrochemical biosensor takes the polypeptide as a recognition molecule, and establishes the measurement relationship between the electrochemical signal and the object to be detected according to the property of the object to be detected, so as to realize the qualitative or quantitative detection of the object[8]. Detection methods mainly include current method, potential method and impedance method. In this paper, the applications of peptide-based electrochemical sensors in the detection of heavy metal ions, small molecules, proteins, bacteria and viruses in the past five years are reviewed, and the detection principles and innovations are discussed in order to provide reference for the development and application of peptide-based biosensors. It should be noted that peptide nucleic acids (PNA) are a class of DNA analogues in which glycine replaces the pentose-phosphate backbone in nucleic acids, and have been widely used in nucleic acid sensing assays[9]. The application of peptide nucleic acid (PNA) biosensing analysis is not reviewed in this paper.

3.1 Recognition and Detection of Heavy Metal Ions

The presence of heavy metal ions such as cadmium and lead in the environment can cause serious water pollution and even endanger human health through the transfer of the food chain. Researchers have designed and synthesized a variety of chemical probes to recognize specific heavy metal ions, including fluorescent probes and ionophores. In addition, as shown in Figure 2, the researchers designed, screened and synthesized a variety of selective recognition polypeptides for heavy metal ions[10⇓⇓⇓~14]. Electrochemical sensors based on peptide recognition can be used to detect heavy metal ions such as Zn2+, Cu2+, Hg2+, Pb2+ and Ag+.
In the past five years, the related research work mainly focused on the detection of Zn2+, Cu2+ and Pb2+. Miao et al. Used [Fe(CN)6]3-/4- as redox probe to indicate the specific capture of Zn2+ by cysteine in immobilized polypeptide (CCPGC)[15]. The change of the electrode resistance is linear with the concentration of the Zn2+ in the range of 10-500 nmol/L with a detection limit of 5 nmol/L. Based on the above similar principles, Miao et al. Used polypeptide (GGH) as a specific recognition probe for Cu2+ to realize the electrochemical impedance detection of Cu2+[16]. Based on the binding of various functional groups in peptides (CTNTLSNNC) and glutathione (GSH) with heavy metal ions, the researchers developed square wave voltammetry for the detection of Pb2+ by directly utilizing the redox characteristics of heavy metal ions[17,18]. In order to improve the stability and reproducibility of electrochemical analysis, a ratiometric electrochemical sensor based on neurokinin B (NKB) was designed for the specific detection of Cu2+[19]. NKB is modified on the surface of the electrode with 2,2 '-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) through the covalent bond of glutaraldehyde crosslinking agent, and captures the Cu2+ in the solution to form a [CuII(NKB)2] complex. The detection was achieved by the ratio of the Cu2+ to the peak current of ABTS in differential pulse voltammetry with a detection limit of 40 nmol/L.
As a hydrophilic recognition molecule, polypeptide is usually difficult to be used as a carrier in the field of ion selective electrode potential analysis. Gyurcsanyi's group combined metal-binding peptide as hydrophilic ionophore with nanopore to construct a potentiometric sensor for specific detection of Cu2+[10]. The polypeptide is modified on the surface of the nanoporous electrode through an Au-S bond and is used as a carrier to form a four-ligand complex with a Cu2+, thereby regulating the change of electrode potential. The electrode is sensitive to Ca2+, Zn2+, Cd2+, Pb2+,The selectivity coefficients ( log K Cu , J pot) of the Na+ were -3.63, -4.26, -3.19, -3.08 and -5.56, respectively. The Nernst linear response range of the electrode is 10-3~10-6mol/L. By designing suitable polypeptide sequences, the method can expand the application of the polypeptide in the field of potential sensing analysis. It should be pointed out that the application of peptide-based electrochemical sensing in heavy metal ion detection is still limited. In addition, compared with traditional chemical ligands such as ionophores, the binding specificity of peptides to heavy metal ions and the sensitivity of electrode detection need to be further improved[20].

3.2 Recognition and detection of small molecules

Highly sensitive detection of small molecular substances is an urgent need in the fields of environmental monitoring, food quality and safety, and medicine. At present, a variety of polypeptide sequences have been developed for the detection of small gas molecules, such as volatile gases in chocolate (such as acetic acid, nonenoic acid, acetyl pyrrole, methyl butyraldehyde), volatile gases in water or fruit juice (such as n-butanol, n-hexanol, ethanolamine, etc.), and long-chain aldehydes (such as octanal, decanal, undecanal, nonanal and new heliotropin)[21][22][23].
In recent years, peptide-based electrochemical sensors have focused on the detection of hydrogen peroxide in the field of small molecule detection. The detection of hydrogen peroxide with high sensitivity and accuracy is of great significance in the fields of food industry, biology, clinical control and environmental protection. The nano composite constructed by combining the polypeptide with the graphene quantum dots, the nano gold or the nano silver can improve the sensitivity of H2O2 detection. Wei et al. Connected a new functional peptide (AEAKAEAKYWYAFAEAKAEAK) nanofiber with graphene quantum dots and graphene oxide[24]. The H2O2 was detected by cyclic voltammetry, and the linear range was 1.0×10-5~7.2×10-3mol/L. Graphene oxide-peptide-gold nanohybrids were constructed based on a peptide with the sequence FEFEFKFK, and dipeptide (FF) was used to functionalize graphene oxide to form nanofibers with gold nanoparticles using hydrophobic interactions between the specific domains of the peptide (CCYAEAKAEAKAEAKAKAKRGD). The researchers developed voltammetry for the detection of H2O2 with detection limits of 0.13, 0.10 and 3.43 μmol/L, respectively[25][26][27].
2,4,6-Trinitrotoluene (TNT) is the main component of dangerous explosives. Toko et al. Made a functional chip using a microelectrode modified by a polypeptide (ARGYSSFIYWFFDFC), which realized the rapid and real-time detection of TNT molecules[28]. The polypeptide has a negative charge, and when the TNT molecule interacts with the peptide through pi-pi and hydrogen bonding, charge transfer occurs between the positively charged group in the TNT molecule and the negatively charged peptide, resulting in a potential change. The linear range was 8. 4 ~ 276.1 μmol/L, and the detection limit was 2. 6 μmol/L.

3.3 Identification and detection of protein

There are three main modes of protein recognition by polypeptides (Fig. 3): (1) polypeptide-specific recognition of binding proteins, such as Tau protein, human immunoglobulin, Toxoplasma immunoglobulin and amyloid protein; (2) protein specifically recognize and cleaves polypeptide, such as matrix metalloproteinase, trypsin, caspase, cathepsin, etc.; (3) that substrate polypeptide is phosphorylate by a protease, such as a protein kinase. Peptide-based electrochemical sensors have been used for the qualitative and quantitative detection of a variety of proteins, and their polypeptide sequences and sensor performance are shown in Table 1.

3.3.1 Peptide and protein specific recognition and binding

The detection principles of electrochemical sensors based on the specific recognition and binding of peptides and proteins mainly include four kinds: (1) the binding of peptides and proteins prevents the electrochemical probe from approaching the electrode surface, resulting in changes in signal current, impedance, etc.; (2) that conformation of the polypeptide or the protein is Chan due to the specific recognition and combination of the polypeptide and the protein, so that the electrochemical signal is changed; (3) detection technology base on specific recognition of target protein to induce peptide chain displacement reaction; (4) "Sandwich" electrochemical sensing technology based on the combination of polypeptide and protein.
Based on the blocking effect of peptide binding to protein, the researchers used [Fe(CN)6]3-/4- as an indicator probe, immobilized specific recognition peptides, and used square wave voltammetry and electrochemical impedance spectroscopy to detect neutrophil gelatinase-associated lipocalin, leucine-rich alpha-glycoprotein 1, cardiac troponin I and metalloproteinase[29][30][31][32]. In order to improve the sensitivity of the assay, Park et al. Immobilized peptide display phage on the surface of gold electrode to specifically capture the NS1 protein of dengue virus[33]. Compared with a single affinity peptide sensor, each phage surface of the sensor has five copies of the NS1 protein to recognize the peptide, thereby enhancing the protein-polypeptide interaction and reducing the detection limit based on impedance analysis to 0.025 μg/mL. In addition, the researchers used the interaction between gold nanoparticles or silver nanoparticles in solution and the peptides assembled layer by layer on the electrode surface to regulate the resistance of the electrode surface to improve the sensitivity of the analytical test, and the detection limits for human chorionic gonadotropin were 0. 6 and 0. 4 mIU/mL, respectively[34,35].
Based on the hindrance effect caused by the binding of peptides to proteins, researchers have also developed electrochemical sensors for a variety of proteins using electroactive substances such as silver nanoparticles, ferrocene and methylene blue as indicator signals[36][37][38]. To improve the antifouling performance of the sensor, Luo et al. designed a multifunctional peptide containing an anchoring domain, an antifouling domain, and a specific recognition domain for the target molecule (fig. 4)[39]. In this study, the redox signal of polyaniline (PANI) was used as an indicator to detect IgG in pure serum and clinical samples by differential pulse voltammetry. In addition, using CdS quantum dots as photoelectrically active substances, Damos et al. Developed a photoelectrical detection technique for Mycobacterium leprae antibodies in human serum samples based on the reduction of the efficiency of hole transfer from photoelectrically active substances to donor molecules and the reduction of photocurrent caused by the specific capture of antibodies by recombinant peptide mimics[40].
Based on the conformational change of polypeptide or protein caused by the binding of polypeptide and protein, researchers have developed a variety of electrochemical sensors for protein detection[41⇓~43]. Brito-Madurro et al. used polypeptides to capture Toxoplasma gondii immunoglobulin, thus changing the tertiary structure of the immunoglobulin and exposing some amino acid residues[41]. By using the [Fe(CN)6]3-/4- as a redox probe, the method realizes the specific detection of the Toxoplasma gondii immunoglobulin in a mouse serum sample. The researchers also realized the detection of arthritis-related specific immunoglobulins based on the change of the conformation of polypeptides after specific capture of the analyte, which leads to the change of redox current of oxidizable amino acids in the polypeptide chain[43].
Liu et al. Designed a biosensor for the specific detection of Tau protein based on the peptide chain displacement reaction induced by the binding of polypeptide to protein (fig. 5)[44]. Heptapeptide (1, 1 ') can form a helical coil through the electrostatic and hydrophobic interaction of amino acids, and combine with the specific recognition peptide 2 of Tau protein to modify the electrode surface as a substrate for displacement reaction. In order to realize the peptide chain displacement reaction, the 1 '-2' chain of the modified ferrocene redox probe was used as the initiator, in which the peptide segment 2 'could specifically recognize and bind with the peptide segment 2. In the absence of Tau protein, the initiator can completely replace the chain 1 'to bind to the electrode surface and generate an electrochemical signal. When Tau protein is present, the binding of the initiator to Tau protein results in the inability of ferrocene to access the electrode surface. In this study, differential pulse voltammetry was used to detect Tau protein with a detection limit of 0. 3 nmol/L. The detection limit and linear range of the product were the same as those of pure Tau protein, although the electrochemical response signal was weakened by the influence of complex matrix in human serum samples.
Based on the combination of peptides and proteins, researchers have developed a variety of "sandwich" electrochemical sensor technologies. "Sandwich" conjugates have been reported to include polypeptide-protein-antibody, antibody-protein-peptide display phage, polypeptide-protein-nucleic acid aptamer, and polypetide-antibody-protein, among others. De-Simone et al. Immobilized the polypeptide on the surface of the electrode to specifically recognize and bind the spotted fever pathogen-Rickettsia antibody, and formed a "sandwich" structure with alkaline phosphatase as the enzyme label[45]. In this study, the detection of Rickettsia antibody was realized based on the current signal generated by the substrate catalyzed by the enzyme. The researchers also developed a "sandwich" peptide electrochemical detection technique using horseradish peroxidase as the enzyme label[46,47]. Zhang et al. Realized the quantitative detection of cardiac troponin I (cTnI) by constructing a "sandwich" immunoreaction based on aptamer (S1) through self-assembled peptides[48]. In this study, the auxiliary DNA was introduced to form double-stranded DNA with aptamer, so that the photoelectric active substance Ru (III) ) 3 2 + could be embedded into double-stranded DNA to generate optical signals. Yang et al. Constructed a "sandwich" photocurrent assay for human epidermal growth factor receptor 2 (HER2) by combining polypeptide with aptamer and using the characteristic that Na2MoO4 can react with the phosphate group of aptamer to form phosphomolybdate precipitate, which hinders the electron transfer of photoactive material-hexagonal carbon nitride tube[49].

3.3.2 Proteins specifically recognize and cleave a polypeptide

The detection principle of the electrochemical sensor based on protein cleavage polypeptide is as follows: one end of a peptide chain is modified with an enzyme or a redox probe, such as horseradish peroxidase, ferrocene, methylene blue and the like, and the peptide chain is cleaved to cause the release of the enzyme or the probe, thereby causing the change of an electrochemical signal; Or [Fe(CN)6]3-/4-, AgNPs and the like are used as redox signal indication, and the indirect electrochemical detection of the protein is realized through the change of the indication signal after the polypeptide is cut by the protein.
Ma et al. Used PSA to cut the immobilized polypeptide on the electrode surface, and used methylene blue (MB) or Pb2[Fe(CN)6] as redox probes to achieve specific detection of prostate specific antigen (PSA)[50,51]. In addition, the polypeptide can realize the quantitative detection of various proteases through the signal indication of electrostatic assembly of AgNPs or chain end modification of horseradish peroxidase, thionine, methylene blue, ferrocene and the like[52][53][54][55⇓~57][58]. CdTe quantum dots and peptides were immobilized on the electrode surface by electrostatic adsorption, and photocurrent-based tyrosinase and thrombin biosensors were developed[59].
In addition, researchers have developed an electrochemiluminescence sensor for specific detection of proteases based on target-induced polypeptide cleavage strategy[60,61]. CdS quantum dots on the surface of the electrode are used as an electrochemiluminescence emission source, and ferrocene modified at the end of the peptide is used as a quencher; Or adriamycin-luminol is used as a luminophore, dissolved oxygen is used as an endogenous synergistic activator, and the Au-Ag-Pt heterogeneous nanostructure is used as a co-reaction promoter. Based on the change of electrochemical signal caused by the cleavage of metalloprotease, the quantitative detection of target protein can be realized. Based on the hydrolysis resistance of acetylated peptides and the characteristics of tannic acid assembled gold nanoprobe mimicking superoxide dismutase (SOD), the researchers designed an electrochemiluminescence sensor for specific detection of histone acetyltransferase activity[62].

3.3.3 The polypeptide is phosphorylated or acetylated by a protease

The phosphorylation or acetylation of a specific sequence of polypeptides can bind to a specific substance, thereby causing a change in certain electrical quantities. The LRRASLG fragment in the polypeptide sequence is an ideal substrate for phosphorylation catalyzed by protein kinase A. Based on the combination of Zr4+ and phosphate, this study can detect the activity of PKA by connecting a large number of ferrocene labels to phosphorylation sites through Zr4+ or designing peptide-copper nanoparticle probes based on voltammetry[63][64]. Ai et al designed a Photoelectrochemical sensor for the specific detection of protein kinase by using the ability of phosphate to bond with TiO2 and photoactive material graphite carbonitride (g-C3N4)[65].
In addition, acetyl groups can modify the peptide chain under the action of acetyltransferase. For example, in the presence of HAT P300, the acetyl group can be transferred from acetyl-Coa to the lysine of the polypeptide. Therefore, graphene oxide nanolayers containing acetylated antibody (AbAc) and a large amount of methylene blue can be modified on the surface of the electrode through the recognition of AbAc and acetyl groups, resulting in electrochemical signals. Peng et al. Designed a sensitive electrochemical immunosensor for the specific detection of histone acetyltransferase (HAT P300) based on this principle[66]. The detection limit of this method is 3.6 pmol/L.

3.4 Identification and detection of bacteria and virus

Antimicrobial peptides have unique advantages in the recognition of multiple pathogenic bacteria because they can act on a certain bacterium semi-selectively or highly selectively[67]. Peptides in the natural immune system and synthetic antimicrobial peptides have the advantages of wide distribution, low toxicity and multiple binding sites on the surface of bacteria. Polypeptides are smaller and more biologically stable than antibodies or DNA. Qin et al. split the antimicrobial peptide (WGEAFSAGVHRLAN) into two fragments as a "sandwich" recognition molecule pair, and used streptavidin magnetic beads for magnetic separation to achieve specific detection of Listeria monocytogenes (LM) (Figure 6)[68]. Horseradish peroxidase can catalyze the substrate 3,3 ', 5,5' -tetramethylbenzidine to form positively charged intermediates, such as free radicals, charge transfer complexes and diimines, resulting in a large potential response on the surface of polymer sensitive membrane ion-selective electrode containing ion exchanger, with a detection limit of 10 CFU/mL.
Peptide-based electrochemical sensing for the detection of pathogens is mainly based on the change of electrochemical impedance before and after the binding of pathogens. By immobilizing the antibacterial peptide colicin (ColV) and helicine (Clavanin A sequence is VFQFLGKIIHHVGNFVHGFSHVF) on the surface of the electrode, and using [Fe(CN)6]3-/4- as redox probe, the detection of various pathogenic bacteria can be realized by cyclic voltammetry or impedance method, and can be used to selectively distinguish Gram-positive bacteria from Gram-negative bacteria[69][70⇓~72]. Gil et al. Combined the miniature integrated impedance sensor with antimicrobial peptides for quantitative detection of Streptococcus sanguis. The linear range was 10~1.0×105CFU/mL and the detection limit was 3.5 CFU/mL[73].
Viruses consist of a protein coat and internal genetic material. As a recognition molecule, that polypeptide can realize the specific recognition of the virus surface protein. Park et al. Modified the gold electrode with a peptide (EHDRMHAYYLTRGGGGSC) to capture dengue virus (DENV) surface antigen (NS1), and used ferrocene as a redox probe to realize the specific detection of DENV in clinical serum samples by square wave voltammetry[74]. Ito et al. inserted a 3,4-ethylenedioxythiophene (EDOT) monomer into a polypeptide (ARRBGHRKPRR) sequence and dispersed it in a solution to capture influenza virus[75]. The binding of the polypeptide to the influenza virus hinders the electropolymerization of EDOT on the electrode surface, thereby changing the redox current of the [Fe(CN)6]3-/4- probe. In this study, the virus was detected by changing the peak current of cyclic voltammetry. The linear range of the sensor was 12. 5 ~ 100 μg/mL, and the detection limit was 12. 5 μg/mL. The protein coat of the virus is insulating, and the peptide-based electrochemical sensor can also detect the virus by utilizing the change of electrochemical impedance before and after the virus is combined with the polypeptide. Park et al modified the polypeptide (QHKMHKPHKNTKEKEK EKEGGGGSGGGGSC) on the surface of gold nanoparticles, and used [Fe(CN)6]3-/4- as redox probe to achieve specific detection of Norwalk virus by electrochemical impedance spectroscopy, with a detection limit of 2. 37 copies/mL[76]. Based on the above electrochemical impedance principle, Sato et al. Realized the quantitative detection of influenza virus (IFV) using sialic acid carbohydrate mimetic peptide (ARLPR)[77,78]. The linear range of the biosensor for H1N1 and H3N2 was 20-500 pfu, and the detection limits were 3. 3 and 0. 91 pfu, respectively.
It should be pointed out that at present, antimicrobial peptides usually act semi-selectively on a certain pathogen. Therefore, it is of great significance to develop electrochemical sensor arrays using peptides as recognition molecules and explore their rapid screening strategies in a variety of pathogens. In addition, it is also an important research direction to develop new recognition sequences to improve the specific recognition of peptides to pathogens by targeting the membrane proteins on the surface of pathogens.

4 Conclusion and prospect

Peptide-based electrochemical sensors and their analytical applications to ions, small molecules, proteins, bacteria and viruses are reviewed in this paper, which provides a reference for future research on peptide-based sensing systems. With the development of peptide design, screening and synthesis methods, and the wide application of new electrochemical principles, new technologies and new materials, peptide-based electrochemical sensors will be more studied and applied. Screening polypeptide recognition sequences with higher selectivity, such as changing the type, number and sequence of amino acids to improve the selectivity; Functional design of polypeptide and DNA-polypeptide composite molecules with new conformation and structure to construct new biomaterials and sensing interfaces based on molecular self-assembly; Development of new electrochemical signal amplification technologies based on nanomaterials and biotechnology; Exploring new principles and methods of electrochemical sensing to improve the biosensing performance of peptides[79]; The design of sensor arrays to achieve the simultaneous detection of multiple substances to be detected is an important development direction of polypeptide sensing systems in the future. In addition, it is very important to develop more application systems for the application of laboratory detection technology to actual sample analysis and testing, such as real-time monitoring of the analyte in living cells by improving the biocompatibility of polypeptides; The multifunctional polypeptide is adopted to reduce non-specific adsorption and improve the anti-fouling ability of the sensor.

References

Publishing order | Descend order by publishing year | Descend order by cited within
[1]

Cui Y, Kim S N, Naik R R, McAlpine M C. Acc. Chem. Res., 2012, 45(5): 696.
[2]

Karimzadeh A, Hasanzadeh M, Shadjou N, Guardia M D L. Trac Trends Anal. Chem., 2018, 107: 1.
[3]

Liu Q T, Wang J F, Boyd B J. Talanta, 2015, 136: 114.
[4]

Lowman H B. Annu. Rev. Biophys. Biomol. Struct., 1997, 26(1): 401.
[5]

Barbosa A J M, Oliveira A R, Roque A C A. Trends Biotechnol., 2018, 36(12): 1244.
[6]

Pavan S, Berti F. Anal. Bioanal. Chem., 2012, 402(10): 3055.
[7]

Wang Z X, Wang Y F, Qi W, Su R X, He Z M. Prog. Chem., 2020, 32: 687.
[8]

( 王子瑄, 王跃飞, 齐崴, 苏荣欣, 何志敏. 化学进展, 2020, 32: 687.).
[9]

Puiu M, Bala C. Bioelectrochemistry, 2018, 120: 66.
[10]

Saadati A, Hassanpour S, Guardia M D L, Mosafer J, Hashemzaei M, Mokhtarzadeh A, Baradaran B. Trac Trends Anal. Chem., 2019, 114: 56.
[11]

Papp S, Jágerszki G, Gyurcsányi R E. Angew. Chem. Int. Ed., 2018, 57(17): 4752.
[12]

Thirupathi P, Lee K H. Bioorg. Med. Chem. Lett., 2013, 23: 6811.
[13]

Jung K H, Oh E T, Park H J, Lee K H. Biosens. Bioelectron., 2016, 85: 437.
[14]

Kim J M, Lohani C R, Neupane L N, Choi Y, Lee K H. Chem. Commun., 2012, 48(24): 3012.
[15]

Neupane L N, Oh E T, Park H J, Lee K H. Anal. Chem., 2016, 88(6): 3333.
[16]

Liu T, Yin J, Wang Y H, Miao P. J. Electroanal. Chem., 2016, 783: 304.
[17]

Jiang Y, Chen X F, Lan L T, Pan Y, Zhu G X, Miao P. New J. Chem., 2018, 42(18): 14733.
[18]

Jiang M, Chen H R, Li S S, Liang R, Liu J H, Yang Y, Wu Y J, Yang M, Huang X J. Environ. Sci.: Nano, 2018, 5(11): 2761.
[19]

Lin M, Cho M, Choe W S, Lee Y. Electroanalysis, 2016, 28(5): 998.
[20]

Yu Y Y, Wang P, Zhu X D, Peng Q W, Zhou Y, Yin T X, Liang Y X, Yin X X. Anal., 2018, 143(1): 323.
[21]

Ding J W, Qin W. Trac Trends Anal. Chem., 2020, 124: 115803.
[22]

Compagnone D, Faieta M, Pizzoni D, Di Natale C, Paolesse R, van Caelenberg T, Beheydt B, Pittia P. Sens. Actuat. B: Chem., 2015, 207: 1114.
[23]

Mascini M, Gaggiotti S, Della Pelle F, di Natale C, Qakala S, Iwuoha E, Pittia P, Compagnone D. Front. Chem., 2018, 6: 105.
[24]

Wasilewski T, Szulczyński B, Wojciechowski M, Kamysz W, Gębicki J. Microchem. J., 2020, 154: 104509.
[25]

Li Y, Zhang W S, Zhang L, Li J F, Su Z Q, Wei G. Adv. Mater. Interfaces, 2017, 4(3): 1600895.
[26]

Wang L, Lin J. Appl. Sci., 2017, 9: 160.
[27]

Wu Y J, Wang F, Lu K, Lv M, Zhao Y F. Sens. Actuat. B: Chem., 2017, 244: 1022.
[28]

Zhang W S, Xi J D, Zhang Y C, Su Z Q, Wei G. Arab. J. Chem., 2020, 13(1): 1406.
[29]

Wang J, Yatabe R, Onodera T, Tanaka M, Okochi M, Toko K. Sens. Mater., 2019, 31(8): 2609.
[30]

Cho C H, Kim J H, Song D K, Park T J, Park J P. Biosens. Bioelectron., 2019, 142: 111482.
[31]

Lim J M, Ryu M Y, Yun J W, Park T J, Park J P. Biosens. Bioelectron., 2017, 98: 330.
[32]

Wang B, Jing R, Qi H L, Gao Q, Zhang C X. J. Electroanal. Chem., 2016, 781: 212.
[33]

Ma F, Yan J D, Sun L N, Chen Y. Talanta, 2019, 205: 120142.
[34]

Lim J M, Kim J H, Ryu M Y, Cho C H, Park T J, Park J P. Anal. Chimica Acta, 2018, 1026: 109.
[35]

Xia N, Wang X, Yu J, Wu Y Y, Cheng S C, Xing Y, Liu L. Sens. Actuat. B: Chem., 2017, 239: 834.
[36]

Xia N, Wang X, Yu J, Wu Y Y, Chen S C, Xing Y, Liu L. Sens. Actuat. B: Chem., 2017, 243: 784.
[37]

Xing Y, Feng X Z, Zhang L P, Hou J T, Han G C, Chen Z C. Int. J. Nanomed., 2017, 12: 3171.
[38]

Valencia D P, Dantas L M F, Lara A, García J, Rivera Z, Rosas J, Bertotti M. J. Electroanal. Chem., 2016, 770: 50.
[39]

Mahshid S S, Mahshid S, VallÉe-BÉlisle A, Kelley S O. Anal. Chem., 2019, 91(8): 4943.
[40]

Liu N Z, Hui N, Davis J J, Luo X L. ACS Sens., 2018, 3(6): 1210.
[41]

Neto S Y, Lima M I S, Pereira S R F, Goulart L R, Luz R D S, Damos F S. Biosens. Bioelectron., 2019, 143: 111652.
[42]

Alves L M, Barros H L S, Flauzino J M R, Guedes P H G, Pereira J M, Fujiwara R T, Mineo T W P, Mineo J R, de Oliveira R J, Madurro J M, G Brito-Madurro A. J. Pharm. Biomed. Anal., 2019, 175: 112778.
[43]

Negahdary M, Heli H. Microchim. Acta, 2019, 186: 766.
[44]

Rodovalho V R, Araujo G R, Vaz E R, Ueira-Vieira C, Goulart L R, Madurro J M, Brito-Madurro A G. Biosens. Bioelectron., 2018, 100: 577.
[45]

Dai Y F, Abbasi K, Bandyopadhyay S, Liu C C. ACS Sens., 2019, 4(8): 1980.
[46]

Prado I C, Chino M E T A, dos Santos A L, Souza A L A, Pinho L G, Lemos E R S, De-Simone S G. Biosens. Bioelectron., 2018, 100: 115.
[47]

Lu X, Jiang D J, Yan J X, Ma Z E, Luo X E, Wei T L, Xu Y, He Q H. Talanta, 2018, 179: 646.
[48]

Vural T, Yaman Y T, Ozturk S, Abaci S, Denkbas E B. J. Colloid Interface Sci., 2018, 510: 318.
[49]

Liu X, Liu H W, Li M, Qi H L, Gao Q, Zhang C X. ChemElectroChem, 2017, 4(7): 1708.
[50]

Luo J J, Liang D, Qiu X Q, Yang M H. Anal. Bioanal. Chem., 2019, 411(26): 6889.
[51]

Tang Z, Fu Y, Ma Z. Biosens. Bioelectron., 2017, 92: 577.
[52]

Tang Z, Fu Y, Ma Z. Biosens. Bioelectron., 2017, 94: 394.
[53]

Song S, Hu X J, Li H J, Zhao J L, Koh K, Chen H X. Sens. Actuat. B: Chem., 2018, 274: 54.
[54]

Khalilzadeh B, Charoudeh H N, Shadjou N, Mohammad-Rezaei R, Omidi Y, Velaei K, Aliyari Z, Rashidi M R. Sens. Actuat. B: Chem., 2016, 231: 561.
[55]

Xu W J, Jing P, Yi H Y, Xue S Y, Yuan R. Sens. Actuat. B: Chem., 2016, 230: 345.
[56]

Gonzalez-Fernandez E, Avlonstis N, Murray A F, Mount A R, Bradley M. Biosens. Bioelectron., 2016, 84: 82.
[57]

Ucar A, González-Fernández E, Staderini M, Avlonitis N, Murray A F, Bradley M, Mount A R. Anal., 2020, 145(3): 975.
[58]

Staderini M, González-Fernández E, Murray A F, Mount A R, Bradley M. Sens. Actuat. B: Chem., 2018, 274: 662.
[59]

Song Y, Fan H F, Anderson M J, Wright J G, Hua D H, Koehne J, Meyyappan M, Li J. Anal. Chem., 2019, 91(6): 3971.
[60]

Chen J X, Liu Y F, Zhao G C. Sensors, 2016, 16(1): 135.
[61]

Nie Y M, Zhang P, Wang H J, Zhuo Y, Chai Y Q, Yuan R. Anal. Chem., 2017, 89(23): 12821.
[62]

Wu F F, Zhou Y, Zhang H, Yuan R, Chai Y Q. Anal. Chem., 2018, 90(3): 2263.
[63]

Zou Y, Wang Z H, Zhang H X, Liu Y. Biosens. Bioelectron., 2018, 122: 205.
[64]

Hu Q, Kong J M, Han D X, Bao Y, Zhang X J, Zhang Y W, Niu L. Talanta, 2020, 206: 120173.
[65]

Zhao J, Yang L L, Dai Y H, Tang Y Y, Gong X Q, Du D S, Cao Y. Biosens. Bioelectron., 2018, 119: 42.
[66]

Wang Y, Li X, Waterhouse G I N, Zhou Y L, Yin H S, Ai S Y. Talanta, 2019, 196: 197.
[67]

Xu L H, Zhang Q Q, Hu Y F, Ma S H, Hu D D, Wang J, Rao J J, Guo Z Y, Wang S, Wu D, Liu Q, Peng J Q. Anal. Chimica Acta, 2019, 1066: 28.
[68]

Etayash H, Jiang K R, Thundat T, Kaur K. Anal. Chem., 2014, 86(3): 1693.
[69]

Lv E, Ding J W, Qin W. Anal. Chem., 2018, 90(22): 13600.
[70]

Jiang K R, Etayash H, Azmi S, Naicker S, Hassanpourfard M, Shaibani P M, Thakur G, Kaur K, Thundat T. Anal. Methods, 2015, 7(23): 9744.
[71]

Andrade C A S, Nascimento J M, Oliveira I S, de Oliveira C V J, de Melo C P, Franco O L, Oliveira M D L. Colloids Surf. B: Biointerfaces, 2015, 135: 833.
[72]

Silva A G Jr, Oliveira M D L, Oliveira I S, Lima-Neto R G, Sá S R, Franco O L, Andrade C A S. Sens. Actuat. B: Chem., 2018, 255: 3267.
[73]

de Miranda J L, Oliveira M D L, Oliveira I S, Frias I A M, Franco O L, Andrade C A S. Biochem. Eng. J., 2017, 124: 108.
[74]

Hoyos-NoguÉs M, Brosel-Oliu S, Abramova N, Muñoz F X, Bratov A, Mas-Moruno C, Gil F J. Biosens. Bioelectron., 2016, 86: 377.
[75]

Kim J H, Cho C H, Ryu M Y, Kim J G, Lee S J, Park T J, Park J P. PLoS One, 2019, 14: 0222144.
[76]

Tara Bahadur K C, Tada S, Zhu L P, Uzawa T, Minagawa N, Luo S C, Zhao H C, Yu H H, Aigaki T, Ito Y. Chem. Commun., 2018, 54(54): 7542.
[77]

Baek S H, Park C Y, Nguyen T P, Kim M W, Park J P, Choi C, Kim S Y, Kailasa S K, Park T J. Food Control., 2020, 114: 107225.
[78]

Matsubara T, Ujie M, Yamamoto T, Akahori M, Einaga Y, Sato T. PNAS, 2016, 113(32): 8981.
[79]

Matsubara T, Ujie M, Yamamoto T, Einaga Y, Daidoji T, Nakaya T, Sato T. ACS Sens., 2020, 5(2): 431.
[80]

Wang L, Zhang Y J, Wu A G, Wei G. Anal. Chim. Acta, 2017, 985: 2.

Funding

National Natural Science Foundation of China(41876108)

Taishan Scholar Program of Shandong Province(tsqn201909163)

Taishan Scholar Program of Shandong Province(tspd20181215)

PDF (7285KB)

2685

Accesses

0

Citation

Detail
Sections
Recommended

/

〈 〉

Address of Editorial Office: No. 33 Beisihuan Xilu, Zhongguancun , Beijing 100190, China
Tel: +86 10 8262 7757
Fax: +86 10 8262 7757
E-mail: progchem@mail.las.ac.cn
http://www.progchem.ac.cn
    • 　
    Copyright © Editorial Office of Progress in Chemistry