Elucidating the mechanism of interaction between peptides and inorganic surfaces

• Published in: Physical chemistry chemical physics : PCCP 2015-06, Vol.17 (23), p.15305-15315
• Main Authors: Maity, Sibaprasad, Zanuy, David, Razvag, Yair, Das, Priyadip, Alemán, Carlos, Reches, Meital
• Format: Article
• Language: English
• Subjects: Amino acids; Binding; Gain; Inorganic materials; Mica; Peptides; Proximity; Simulation
• ISSN: 1463-9076; 1463-9084
• DOI: 10.1039/c5cp00088b

Understanding the mechanism of interaction between peptides and inorganic materials is of high importance for the development of new composite materials. Here, we combined an experimental approach along with molecular simulations in order to gain insights into this binding process. Using single molecule force spectroscopy by atomic force microscopy and molecular simulations we studied the binding of a peptide towards an inorganic substrate. By performing alanine scan we examined the propensity of each amino acid in the peptide sequence to bind the substrate (mica). Our results indicate that this binding is not controlled by the specific sequence of the peptide, but rather by its conformational freedom in solution versus its freedom when it is in proximity to the substrate. When the conformational freedom of the peptide is identical in both environments, the peptide will not adhere to the substrate. However, when the conformational freedom is reduced, i.e., when the peptide is in close proximity to the substrate, binding will occur. These results shed light on the interaction between peptides and inorganic materials.