Advancing Peptide-Based Biorecognition Elements for Biosensors Using in-Silico Evolution
Abstract
Sensors for human health and performance monitoring require biological recognition elements (BREs) at device interfaces for the detection of key molecular biomarkers that are measurable biological state indicators. BREs, including peptides, antibodies, and nucleic acids, bind to biomarkers in the vicinity of the sensor surface to create a signal proportional to the biomarker concentration. The discovery of BREs with the required sensitivity and selectivity to bind biomarkers at low concentrations remains a fundamental challenge. In this study, we describe an in-silico approach to evolve higher sensitivity peptide-based BREs for the detection of cardiac event marker protein troponin I (cTnI) from a previously identified BRE as the parental affinity peptide. The P2 affinity peptide, evolved using our in-silico method, was found to have ∼16-fold higher affinity compared to the parent BRE and ∼10 fM (0.23 pg/mL) limit of detection. The approach described here can be applied towards designing BREs for other biomarkers for human health monitoring.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The specific peptide HWQIAYNEHQWQ exhibits a binding affinity (Kd) of 270 pM comparable to that of antibodies.
“This specific peptide (HWQIAYNEHQWQ) not only exhibits an impressive binding affinity (Kd) of 270 pM comparable to that of antibodies37, but also targets the central portion of cTnI (amino acid residues 114–144) with less susceptibility to proteolysis and is postulated to be an optimal targeting epitope to detect all forms of cTnI present in blood circulation38–40.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [37]
Cites
Clustal W and Clustal X version 2.0
Larkin, M., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., López, R., et al. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm404 · Cited by 28,221 · see citing works
Comparison of multiple Amber force fields and development of improved protein backbone parameters
Horn̆ák, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A. E., & Simmerling, C. L. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,903 · see citing works
I-TASSER: a unified platform for automated protein structure and function prediction
Roy, A., Küçükural, A., & Zhang, Y. (2010) · Nature Protocols · doi:10.1038/nprot.2010.5 · Cited by 6,093 · see citing works
Computed circular dichroism spectra for the evaluation of protein conformation
Greenfield, N. J., & Fasman, G. D. (1969) · Biochemistry · doi:10.1021/bi00838a031 · Cited by 3,697 · see citing works
ZDOCK server: interactive docking prediction of protein–protein complexes and symmetric multimers
Pierce, B. G., Wiehe, K. J., Hwang, H., Kim, B., Vreven, T., & Weng, Z. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu097 · Cited by 1,767 · see citing works
Shape- and Size-Dependent Refractive Index Sensitivity of Gold Nanoparticles
Chen, H., Kou, X., Yang, Z., Ni, W., & Wang, J. (2008) · Langmuir · doi:10.1021/la800305j · Cited by 1,333 · see citing works
Structure of the core domain of human cardiac troponin in the Ca2+-saturated form
Takeda, S., Yamashita, A., Maéda, K., & Maéda, Y. (2003) · Nature · doi:10.1038/nature01780 · Cited by 785 · see citing works
Kalign – an accurate and fast multiple sequence alignment algorithm
Lassmann, T., & Sonnhammer, E. L. L. (2005) · BMC Bioinformatics · doi:10.1186/1471-2105-6-298 · Cited by 701 · see citing works
Zhang, A., & Lieber, C. M. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00608 · Cited by 629 · see citing works
NAMD: a Parallel, Object-Oriented Molecular Dynamics Program
Nelson, M. T., Humphrey, W., Gürsoy, A., Dalke, A., Kalé, L. V., Skeel, R. D., & Schulten, K. J. (1996) · The International Journal of Supercomputer Applications and High Performance Computing · doi:10.1177/109434209601000401 · Cited by 563 · see citing works
Engineered Carbon-Nanomaterial-Based Electrochemical Sensors for Biomolecules
Tiwari, J. N., Vij, V., Kemp, K. C., & Kim, K. S. (2015) · ACS Nano · doi:10.1021/acsnano.5b05690 · Cited by 560 · see citing works
Orendorff, C. J., Gearheart, L. A., Jana, N. R., & Murphy, C. J. (2005) · Physical Chemistry Chemical Physics · doi:10.1039/b512573a · Cited by 465 · see citing works
Real-time measurement of small molecules directly in awake, ambulatory animals
Arroyo‐Currás, N., Somerson, J., Vieira, P. A., Ploense, K. L., Kippin, T. E., & Plaxco, K. W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613458114 · Cited by 458 · see citing works
Advancement and applications of peptide phage display technology in biomedical science
Wu, C., Liu, I.-J., Lu, R., & Wu, H. (2016) · Journal of Biomedical Science · doi:10.1186/s12929-016-0223-x · Cited by 343 · see citing works
Synthesis, Assembly, and Applications of Hybrid Nanostructures for Biosensing
Zhang, S., Geryak, R. D., Geldmeier, J. A., Kim, S., & Tsukruk, V. V. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00088 · Cited by 340 · see citing works
Self-citationHow to Interpret Elevated Cardiac Troponin Levels
Mahajan, V. S., & Jarolı́m, P. (2011) · Circulation · doi:10.1161/circulationaha.111.023697 · Cited by 311 · see citing works
Silicon nanowire biosensors for detection of cardiac troponin I (cTnI) with high sensitivity
Kim, K., Park, C., Kwon, D., Kim, D., Meyyappan, M., Jeon, S., & Lee, J. (2015) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2015.10.008 · Cited by 209 · see citing works
Diversity of Phage-Displayed Libraries of Peptides during Panning and Amplification
Derda, R., Tang, S. K. Y., Li, S. C., Ng, S., Matochko, W. L., & Jafari, M. R. (2011) · Molecules · doi:10.3390/molecules16021776 · Cited by 205 · see citing works
Sánchez-Purrà, M., Carré-Camps, M., de Puig, H., Bosch, I., Gehrke, L., & Hamad‐Schifferli, K. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00110 · Cited by 192 · see citing works
Peptide Phage Display as a Tool for Drug Discovery: Targeting Membrane Receptors
Molek, P., Štrukelj, B., & Bratkovič, T. (2011) · Molecules · doi:10.3390/molecules16010857 · Cited by 188 · see citing works
Kuang, Z., Kim, S. N., Crookes-Goodson, W. J., Farmer, B. L., & Naik, R. R. (2010) · ACS Nano · doi:10.1021/nn901365g · Cited by 184 · see citing works
Self-citationRecent Development of Cardiac Troponin I Detection
Han, X., Li, S., Peng, Z., Othman, A. M., & Leblanc, R. M. (2016) · ACS Sensors · doi:10.1021/acssensors.5b00318 · Cited by 176 · see citing works
Monoclonal Antibody Recognition of Histidine-Rich Peptide Encapsulated Nanoclusters
Slocik, J. M., Moore, J. T., & Wright, D. W. (2002) · Nano Letters · doi:10.1021/nl015706l · Cited by 153 · see citing works
Self-citationTadepalli, S., Kuang, Z., Jiang, Q., Liu, K., Fisher, M. A., Morrissey, J. J., Kharasch, E. D., Slocik, J. M., Naik, R. R., & Singamaneni, S. (2015) · Scientific Reports · doi:10.1038/srep16206 · Cited by 107 · see citing works
Self-citationVogt, S., Su, Q., Gutiérrez‐Sánchez, C., & Nöll, G. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04814 · Cited by 107 · see citing works
Evolution of phage display: from bioactive peptides to bioselective nanomaterials
Petrenko, V. A. (2008) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.5.8.825 · Cited by 103 · see citing works
Determinants of the Detection Limit and Specificity of Surface-Based Biosensors
de Ávila, B. E., Watkins, H. M., Pingarrón, J. M., Plaxco, K. W., Palleschi, G., & Ricci, F. (2013) · Analytical Chemistry · doi:10.1021/ac4012123 · Cited by 97 · see citing works
Electrochemical processes and mechanistic aspects of field-effect sensors for biomolecules
Huang, W., Diallo, A. K., Dailey, J., Besar, K., & Katz, H. E. (2015) · Journal of Materials Chemistry C · doi:10.1039/c5tc00755k · Cited by 95 · see citing works
Aptamer-based Field-Effect Biosensor for Tenofovir Detection
Aliakbarinodehi, N., Jolly, P., Bhalla, N., Miodek, A., Micheli, G. D., Estrela, P., & Carrara, S. (2017) · Scientific Reports · doi:10.1038/srep44409 · Cited by 85 · see citing works
Park, J. P., Cropek, D. M., & Banta, S. A. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22597 · Cited by 84 · see citing works
Fabrication of Anti-human Cardiac Troponin I Immunogold Nanorods for Sensing Acute Myocardial Damage
Zr, G., Gu, C., Fan, X., Bian, Z., Wu, H., Yang, D., Gu, N., & Zhang, J. N. (2009) · Nanoscale Research Letters · doi:10.1007/s11671-009-9415-6 · Cited by 68 · see citing works
High-contrast grating resonators for label-free detection of disease biomarkers
Sun, T., Kan, S., Marriott, G., & Chang-Hasnain, C. J. (2016) · Scientific Reports · doi:10.1038/srep27482 · Cited by 61 · see citing works
Label free nano-aptasensor for interleukin-6 in protein-dilute bio fluids such as sweat
Kumar, L. S. S., Wang, X., Hagen, J., Naik, R., Papautsky, I., & Heikenfeld, J. (2016) · Analytical Methods · doi:10.1039/c6ay00331a · Cited by 59 · see citing works
Self-citationRecent Insights into the Molecular Basis of Muscular Fatigue
Debold, E. P. (2012) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e31824cfd26 · Cited by 57 · see citing works
Clinical implications of the Third Universal Definition of Myocardial Infarction
White, H. D., Thygesen, K. A., Alpert, J. S., & Jaffe, A. S. (2013) · Heart · doi:10.1136/heartjnl-2012-302976 · Cited by 50 · see citing works
Biotic–Abiotic Interactions: Factors that Influence Peptide–Graphene Interactions
Kim, S. S., Kuang, Z., Ngo, Y. H., Farmer, B. L., & Naik, R. R. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b06434 · Cited by 43 · see citing works
Self-citationPlasmonic paper: a porous and flexible substrate enabling nanoparticle-based combinatorial chemistry
Schmucker, A. L., Tadepalli, S., Liu, K., Sullivan, C. J., Singamaneni, S., & Naik, R. R. (2015) · RSC Advances · doi:10.1039/c5ra21977a · Cited by 25 · see citing works
Self-citationXiao, X., Agris, P. F., & Hall, C. K. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/ct5008247 · Cited by 22 · see citing works
Self-citationXiao, X., Agris, P. F., & Hall, C. K. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25021 · Cited by 20 · see citing works
Self-citationTadepalli, S., Kuang, Z., Jiang, Q., et al. (2015) · Scientific Reports · doi:10.1038/srep1620610.1038/srep16206 · Cited by 17 · see citing works
Self-citationXiao, X., Wang, Y., Leonard, J. N., & Hall, C. K. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00714 · Cited by 15 · see citing works
Self-citationRepublished: Clinical implications of the Third Universal Definition of Myocardial Infarction
White, H. D., Thygesen, K. A., Alpert, J. S., & Jaffe, A. S. (2014) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2012-302976rep · Cited by 6 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Achievements and Challenges for Real-Time Sensing of Analytes in Sweat within Wearable Platforms
Brothers, M. C., DeBrosse, M., Grigsby, C. C., Naik, R. R., Hussain, S. M., Heikenfeld, J., & Kim, S. S. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00555 · Cited by 207 · see citing works
Self-citationBiomarkers and Detection Platforms for Human Health and Performance Monitoring: A Review
Sim, J. K., Brothers, M. C., Slocik, J. M., Islam, A. E., Maruyama, B., Grigsby, C. C., Naik, R. R., & Kim, S. S. (2022) · Advanced Science · doi:10.1002/advs.202104426 · Cited by 191 · see citing works
Self-citationPeptide-based electrochemical biosensors utilized for protein detection
Vaňová, V., Mitrevska, K., Milosavljević, V., Hynek, D., Richtera, L., & Adam, V. (2021) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2021.113087 · Cited by 154 · see citing works
The Role of Peptides in the Design of Electrochemical Biosensors for Clinical Diagnostics
Sfragano, P. S., Moro, G., Polo, F., & Palchetti, I. (2021) · Biosensors · doi:10.3390/bios11080246 · Cited by 107 · see citing works
You, J., & Tseng, W. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.05.069 · Cited by 92 · see citing works
Akhlaghi, A. A., Kaur, H., Adhikari, B. R., & Soleymani, L. (2024) · ECS Sensors Plus · doi:10.1149/2754-2726/ad304a · Cited by 86 · see citing works
Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum
Tiambeng, T. N., Roberts, D. S., Brown, K. A., Zhu, Y., Chen, B., Wu, Z., Mitchell, S. D., Guardado-Alvarez, T. M., Jin, S., & Ge, Y. (2020) · Nature Communications · doi:10.1038/s41467-020-17643-1 · Cited by 76 · see citing works
Garg, S., Sachdeva, A., Peeters, M., & McClements, J. (2023) · ACS Sensors · doi:10.1021/acssensors.3c01402 · Cited by 73 · see citing works
Electrochemical Biosensing of Algal Toxins in Water: The Current State-of-the-Art
Zhang, W., Dixon, M., Saint, C. P., Teng, K. S., & Furumai, H. (2018) · ACS Sensors · doi:10.1021/acssensors.8b00359 · Cited by 63 · see citing works
A review on peptide functionalized graphene derivatives as nanotools for biosensing
Joshi, S., Sharma, P., Siddiqui, R., Kaushal, K., Sharma, S., Verma, G., & Saini, A. (2019) · Microchimica Acta · doi:10.1007/s00604-019-3989-1 · Cited by 49 · see citing works
Impact of Self-Assembled Monolayer Design and Electrochemical Factors on Impedance-Based Biosensing
Brothers, M. C., Moore, D. C., Lawrence, M. S., Harris, J., Joseph, R. M., Ratcliff, E. L., Ruiz, O. N., Glavin, N. R., & Kim, S. S. (2020) · Sensors · doi:10.3390/s20082246 · Cited by 48 · see citing works
Self-citationGhasemi, F., & Salimi, A. (2023) · Microchemical Journal · doi:10.1016/j.microc.2023.108432 · Cited by 43 · see citing works
Biosensor platforms for rapid HIV detection
Nandi, S., Mondal, A., Roberts, A., & Gandhi, S. (2020) · Advances in clinical chemistry · doi:10.1016/bs.acc.2020.02.001 · Cited by 39 · see citing works
Wen, X., Ou, Y., Zarick, H. F., Zhang, X., Hmelo, A. B., Victor, Q. J., Paul, E. P., Slocik, J. M., Naik, R. R., Bellan, L. M., et al. (2020) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10165 · Cited by 38 · see citing works
Self-citationReese, H. R., Xiao, X., Shanahan, C. C., Chu, W., Driessche, G. A. V. D., Fourches, D., Carbonell, R. G., Hall, C. K., & Menegatti, S. (2020) · Journal of Chromatography A · doi:10.1016/j.chroma.2020.461237 · Cited by 38 · see citing works
Self-citationChu, W., Prodromou, R., Day, K. N., Schneible, J. D., Bacon, K. B., Bowen, J., Kilgore, R., Catella, C. M., Moore, B., Mabe, M. D., et al. (2020) · Journal of Chromatography A · doi:10.1016/j.chroma.2020.461632 · Cited by 36 · see citing works
Chitosan-Based Biosensor Fabrication and Biosensing Applications
Amirthalingam, S., & Jayakumar, R. (2021) · Advances in polymer science · doi:10.1007/12_2021_85 · Cited by 33 · see citing works
De novo design of peptides that coassemble into β sheet–based nanofibrils
Xiao, X., Wang, Y., Seroski, D. T., Wong, K. M., Liu, R., Paravastu, A. K., Hudalla, G. A., & Hall, C. K. (2021) · Science Advances · doi:10.1126/sciadv.abf7668 · Cited by 31 · see citing works
Self-citationSaviñon-Flores, A. I., Saviñon-Flores, F., Trejo, G., Méndez, E., Ţălu, Ş., González‐Fuentes, M. A., & Méndez‐Albores, A. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.1017305 · Cited by 31 · see citing works
Echeverri, D., & Orozco, J. (2022) · Molecules · doi:10.3390/molecules27238533 · Cited by 31 · see citing works
Chapman, E. A., Roberts, D. S., Tiambeng, T. N., Andrews, J., Wang, M.-D., Reasoner, E. A., Melby, J. A., Li, B. H., Kim, D., Alpert, A. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43321-z · Cited by 28 · see citing works
Giarola, J. D. F., Santos, J., Estévez, M. ‐., Ventura, S., Pallarès, I., & Lechuga, L. M. (2024) · Analytica Chimica Acta · doi:10.1016/j.aca.2024.342559 · Cited by 19 · see citing works
Computational Design of Peptides for Biomaterials Applications
Wang, Y., Stebe, K. J., de la Fuente‐Núñez, C., & Radhakrishnan, R. (2023) · ACS Applied Bio Materials · doi:10.1021/acsabm.2c01023 · Cited by 18 · see citing works
Siddiqui, M. F., Khan, Z. A., & Park, S. (2020) · Nanomaterials · doi:10.3390/nano10061240 · Cited by 18 · see citing works
Patil, P. J., Sutar, S. S., Usman, M. A., Patil, D. N., Dhanavade, M. J., Shehzad, Q., Mehmood, A., Shah, H. A., Teng, C., Zhang, C., et al. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120637 · Cited by 17 · see citing works
Natale, C. D., Battista, E., Lettera, V., Reddy, N., Pitingolo, G., Vecchione, R., Causa, F., & Netti, P. A. (2021) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.1c00146 · Cited by 15 · see citing works
Xiao, X., Sarma, S., Menegatti, S., Crook, N., Magness, S. T., & Hall, C. K. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00743 · Cited by 15 · see citing works
Self-citationXiao, X., Wang, Y., Leonard, J. N., & Hall, C. K. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00714 · Cited by 15 · see citing works
Self-citationZhang, N., Zhu, Y., Li, F., Wang, Y., Fu, Z., Jia, M., Zhan, X., & Zhang, W. (2025) · RSC Advances · doi:10.1039/d5ra04555j · Cited by 14 · see citing works
Xiao, X., Robang, A. S., Sarma, S., Le, J. V., Helmicki, M. E., Lambert, M. J., Guerrero-Ferreira, R., Arboleda-Echavarria, J., Paravastu, A. K., & Hall, C. K. (2022) · PNAS Nexus · doi:10.1093/pnasnexus/pgac263 · Cited by 14 · see citing works
Self-citationRoberts, A., Mahari, S., & Gandhi, S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-824494-4.00007-2 · Cited by 14 · see citing works
In Silico Discovery and Validation of Neuropeptide-Y-Binding Peptides for Sensors
Xiao, X., Kuang, Z., Burke, B. J., Chushak, Y. G., Farmer, B. L., Mirau, P. A., Naik, R. R., & Hall, C. K. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b09439 · Cited by 13 · see citing works
Self-citationDe novo discovery of peptide-based affinity ligands for the fab fragment of human immunoglobulin G
Xiao, X., Kilgore, R., Sarma, S., Chu, W., Menegatti, S., & Hall, C. K. (2022) · Journal of Chromatography A · doi:10.1016/j.chroma.2022.462941 · Cited by 13 · see citing works
Self-citationSarma, S., Herrera, S. M., Xiao, X., Hudalla, G. A., & Hall, C. K. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c03918 · Cited by 12 · see citing works
Self-citationDNA-based molecular recognition system for lactoferrin biosensing
Paziewska−Nowak, A., Urbanowicz, M., Sadowska, K., & Pijanowska, D. G. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.126747 · Cited by 11 · see citing works
Peptide-Functionalized Carbon Nanotube Chemiresistors: The Effect of Nanotube Density on Gas Sensing
Sim, J. K., Huang, T. H., & Kim, S. S. (2023) · Sensors · doi:10.3390/s23208469 · Cited by 11 · see citing works
Self-citationDiscovery of phosphotyrosine-binding oligopeptides with supramolecular target selectivity
Pina, A. S., Morgado, L., Duncan, K., Carvalho, S., Carvalho, H. F., Barbosa, A. J. M., Mariz, B. D. P., Moreira, I. P., Kalafatović, D., Faustino, B. M. M., et al. (2021) · Chemical Science · doi:10.1039/d1sc04420f · Cited by 11 · see citing works
Ni, H., Zhang, L., An, P., Krasavin, A. V., Ali, H., Ni, B., & Chang, J. (2022) · Optics Express · doi:10.1364/oe.446766 · Cited by 11 · see citing works
Guo, W., Wang, J., Guo, W., Kang, Q., & Zhou, F. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03442-0 · Cited by 10 · see citing works
Design of 8-mer peptides that block Clostridioides difficile toxin A in intestinal cells
Sarma, S., Catella, C. M., Pedro, E. T. S., Xiao, X., Durmusoglu, D., Menegatti, S., Crook, N., Magness, S. T., & Hall, C. K. (2023) · Communications Biology · doi:10.1038/s42003-023-05242-x · Cited by 10 · see citing works
Self-citationBicyclic peptide-based assay for uPA cancer biomarker
Moro, G., Sfragano, P. S., Ghirardo, J., Mazzocato, Y., Angelini, A., Palchetti, I., & Polo, F. (2022) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2022.114477 · Cited by 9 · see citing works
Sim, J. K., Kuang, Z., Sant’Anna, G., Krabacher, R., Brothers, M. C., Chávez, J. L., Martin, J. A., Islam, A. E., Maruyama, B., Naik, R. R., et al. (2022) · Advanced Materials Interfaces · doi:10.1002/admi.202201707 · Cited by 9 · see citing works
Self-citationAntigen-Mimic Nanoparticles in Ultrasensitive on-Chip Integrated Anti-p53 Antibody Quantification
Kang, S.-Y., Yuan, D., Barber, R., & Davis, J. J. (2024) · ACS Sensors · doi:10.1021/acssensors.3c02568 · Cited by 8 · see citing works
Muslihati, A., Septiani, N. L. W., Gumilar, G., Nugraha, N., Wasisto, H. S., & Yuliarto, B. (2024) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.3c01965 · Cited by 7 · see citing works
Peptide-Based Electrochemical Nanobiosensors for Clinical Diagnosis
Purohit, B., & Svendsen, W. E. (2023) · Springer eBooks · doi:10.1007/978-981-99-3025-8_9 · Cited by 6 · see citing works
Proteins and peptides voltammetry: Trends, potential, and limitations
Kowalczyk, A., Matysiak-Brynda, E., & Nowicka, A. M. (2018) · Current Opinion in Electrochemistry · doi:10.1016/j.coelec.2018.12.004 · Cited by 6 · see citing works
Chiu, Y.-P., Yadlapalli, B. K., Wang, P., & Chen, W. (2025) · Microchemical Journal · doi:10.1016/j.microc.2025.114744 · Cited by 5 · see citing works
Gao, S., Chen, S., & Lu, Q. (2019) · Langmuir · doi:10.1021/acs.langmuir.8b03898 · Cited by 5 · see citing works
Biosensors for coenzyme A thioester derivatives: Development, optimization and applications
Qiu, J., Bibi, A., Lara, A. R., Wang, Q., & Dai, Z. (2025) · Biotechnology Advances · doi:10.1016/j.biotechadv.2025.108767 · Cited by 4 · see citing works
Catella, C. M., Sarma, S., Hinesley, C. M., Febo, C. E., Breau, K. A., Durmusoglu, D., Purnell, E. F., Magness, S. T., Hall, C. K., Menegatti, S., et al. (2025) · Biotechnology and Bioengineering · doi:10.1002/bit.70102 · Cited by 2 · see citing works
Self-citationJauhar, M. M., Damairetha, F. R., Mardliyati, E., Ulum, M. F., Syaifie, P. H., Fahmi, F., Satriawan, A., Shalannanda, W., & Anshori, I. (2024) · PLoS ONE · doi:10.1371/journal.pone.0305770 · Cited by 2 · see citing works
Sim, J. K., Huang, T. H., Naik, R. R., & Kim, S. S. (2021) · International Conference on Solid-State Sensors, Actuators and Microsystems · doi:10.1109/transducers50396.2021.9495588 · Cited by 2 · see citing works
Self-citationBrothers, M. C., Sim, J. K., Sant’Anna, G., Giordano, A. N., Rao, R. S., Bedford, N. M., & Kim, S. S. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c14021 · Cited by 1 · see citing works
Self-citationProgress in (Photo)electrochemical Biosensors for the Detection of Amyloid-Beta Oligomer
Huang, Y., Wang, N., Yi, X., & Xia, N. (2026) · Biosensors · doi:10.3390/bios16060349 · Cited by 1 · see citing works
Watkins, Z., McHenry, A., & Heikenfeld, J. C. (2023) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2023_238 · Cited by 1 · see citing works
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
Dragulska, S. A., Wlodarczyk, M. T., Poursharifi, M., Martignetti, J. A., & Mieszawska, A. J. (2019) · Journal of Visualized Experiments · doi:10.3791/59034
Hall, C. K. (2020) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-101519-120354
Self-citationAutobiography of Carol K. Hall
Hall, C. K. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c07825
Self-citationAdams, V. R., Sarma, S., Hall, C. K., & Kennedy, A. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.12.584666
Self-citationAdvancements in peptide-based gas biosensors
Neubauer, D. (2024) · Comprehensive analytical chemistry · doi:10.1016/bs.coac.2024.11.001
Biosensors for protein and peptide delivery
Priyanka, K., Biswal, S., Parmanik, A., & Sahoo, R. N. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-21592-6.00013-6
Syaifie, P. H., Putri, S. A., Aliya, F., Jauhar, M. M., Wakhid, M. F. R., Mardliyati, E., Siburian, R. A. F., Whulanza, Y., & Anshori, I. (2025) · RSC Advances · doi:10.1039/d5ra04799d
Designed peptides as affinity ligands for extracellular-vesicle-based cancer diagnosis
Sarma, S., Park, J., Cho, Y. K., Tapdiya, A., Woo, H.-K., Lee, H., & Hall, C. K. (2026) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2026.118584
Self-citationSun, Z., Shi, S., Yu, L., Liu, J., 庞月红, & Shen, X. (2026) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2026.141104
- Authors
- Xiao, X., Kuang, Z., Slocik, J. M., Tadepalli, S., Brothers, M., Kim, S., Mirau, P. A., Butkus, C., Farmer, B. L., Singamaneni, S., Hall, C. K., & Naik, R. R.
- Affiliations
- North Carolina State University (US)
- United States Air Force Research Laboratory (US)
- Washington University in St. Louis (US)
- Corresponding author
- Hall, Carol K.
- Naik, Rajesh R.
- ORCID
- Venue
- ACS Sensors
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-05-09
- Volume
- 3
- Issue
- 5
- Pages
- 1024-1031
- ISSN
- 2379-3694 (ISSN-L)
- OpenAlex
- W2800287583
- Cited by
- 65
- References
- 42
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 8 · 2023: 9 · 2022: 11 · 2021: 10 · 2020: 8 · 2019: 6 · 2018: 2 · 2017: 1
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- ACS Sensors (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Air Force Office of Scientific Research (FA9550-15-1-0228, FA9550-16-10078, 12RX11COR)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced biosensing and bioanalysis techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced Biosensing Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- in silico evolution, biosensors, troponin I, cardiac biomarkers, affinity peptides, detection limit, biomarker detection, human health monitoring, protein-peptide interactions
- MeSH terms
- Amino Acid Sequence, Circular Dichroism, Computer Simulation, Humans, Immunoassay, Microscopy, Electron, Scanning, Peptides, Reproducibility of Results, Biosensing Techniques, Biomarkers, Troponin I, Surface Plasmon Resonance, Limit of Detection, Dielectric Spectroscopy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review