ArticleThe journal of physical chemistry letters2019
Monolayer Sensitivity Enables a 2D IR Spectroscopic Immuno-biosensor for Studying Protein Structures: Application to Amyloid Polymorphs.
Article in The journal of physical chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Multidimensional Infrared Spectroscopy as a Bioanalytical Technique.Chemical reviews · 2026Review
- Advances in Probing Amyloid Heterogeneity Using Vibrational Spectroscopy and Imaging.The journal of physical chemistry. B · 2025Review
- Real-Time Monitoring of Chemisorption of Antibodies onto Self-Assembled Monolayers Deposited on Gold Electrodes Using Electrochemical Impedance Spectroscopy.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Development and Characterization of Electrodes for Surface-Specific Attenuated Total Reflection Two-Dimensional Infrared Spectroelectrochemistry.The journal of physical chemistry. C, Nanomaterials and interfaces · 2023Article
- Increasing Pump-Probe Signal toward Asymptotic Limits.The journal of physical chemistry. B · 2023Review
- Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2022Review
- Coupling chemical biology and vibrational spectroscopy for studies of amyloids in vitro and in cells.Current opinion in chemical biology · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Structure Changes of a Membrane Polypeptide under an Applied Voltage Observed with Surface-Enhanced 2D IR Spectroscopy.The journal of physical chemistry letters · 2021Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Immunosensors use antibodies to detect and quantify biomarkers of disease, though the sensors often lack structural information. We create a surface-sensitive two-dimensional infrared (2D IR) spectroscopic immunosensor for studying protein structures. We tether antibodies to a plasmonic surface, flow over a solution of amyloid proteins, and measure the 2D IR spectra. The 2D IR spectra provide a global assessment of antigen structure, and isotopically labeled proteins give residue-specific structural information. We report the 2D IR spectra of fibrils and monomers using a polyclonal antibody that targets human islet amyloid polypeptide (hIAPP). We observe two fibrillar polymorphs differing in their structure at the G24 residue, which supports the hypothesis that hIAPP polymorphs form from a common oligomeric intermediate. This work provides insight into the structure of hIAPP, establishes a new method for studying protein structures using 2D IR spectroscopy, and creates a spectroscopic immunoassay applicable for studying a wide range of biomarkers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.