Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81108
Title: Quantitative Evaluation of Peptide–Material Interactions by a Force Mapping Method: Guidelines for Surface Modification
Authors: Jackman, Joshua Alexander
Mochizuki, Masahito
Oguchi, Masahiro
Kim, Seong-Oh
Ogawa, Tetsu
Lkhamsuren, Ganchimeg
Cho, Nam-Joon
Hayashi, Tomohiro
Keywords: Chemical and Biomedical Engineering
Materials Science and Engineering
Issue Date: 2015
Source: Mochizuki, M., Oguchi, M., Kim, S.-O., Jackman, J. A., Ogawa, T., Lkhamsuren, G., et al. (2015). Quantitative Evaluation of Peptide–Material Interactions by a Force Mapping Method: Guidelines for Surface Modification. Langmuir, 31(29), 8006-8012.
Series/Report no.: Langmuir
Abstract: Peptide coatings on material surfaces have demonstrated wide application across materials science and biotechnology, facilitating the development of nanobio interfaces through surface modification. A guiding motivation in the field is to engineer peptides with a high and selective binding affinity to target materials. Herein, we introduce a quantitative force mapping method in order to evaluate the binding affinity of peptides to various hydrophilic oxide materials by atomic force microscopy (AFM). Statistical analysis of adhesion forces and probabilities obtained on substrates with a materials contrast enabled us to simultaneously compare the peptide binding affinity to different materials. On the basis of the experimental results and corresponding theoretical analysis, we discuss the role of various interfacial forces in modulating the strength of peptide attachment to hydrophilic oxide solid supports as well as to gold. The results emphasize the precision and robustness of our approach to evaluating the adhesion strength of peptides to solid supports, thereby offering guidelines to improve the design and fabrication of peptide-coated materials.
URI: https://hdl.handle.net/10356/81108
http://hdl.handle.net/10220/40648
ISSN: 0743-7463
DOI: 10.1021/acs.langmuir.5b01691
Rights: © 2015 American Chemical Society.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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