Quantitative Evaluation of Peptide–Material Interactions by a Force Mapping Method: Guidelines for Surface Modification

• Published in: Langmuir 2015-07, Vol.31 (29), p.8006-8012
• Main Authors: Mochizuki, Masahito, Oguchi, Masahiro, Kim, Seong-Oh, Jackman, Joshua A, Ogawa, Tetsu, Lkhamsuren, Ganchimeg, Cho, Nam-Joon, Hayashi, Tomohiro
• Format: Article
• Language: English
• Subjects: Hydrophobic and Hydrophilic Interactions; Microscopy, Atomic Force; Peptides - chemistry
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/acs.langmuir.5b01691

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.