Elucidating the Mechanism of Interaction between Peptides and Inorganic Surfaces

Yair Razvag, Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel
Sibaprasad Maity, Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel
carlos Aleman, Chemical Engineering, Universitat Politècnica de Catalunya, Barcelona, Spain
Meital Reches, Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

Composite materials with unique properties such as high mechanical strength, optical functionality or electronic structure are formed in nature through the specific interactions between organic biomolecules, such as protein and peptides and inorganic materials. The specific binding affinity of peptides towards inorganic substrates has been utilized to prepare nanostructured materials with novel properties and functions, such as surface biocompatibility, drug delivery, crystal growth regulation, and nanoparticle synthesis. However, a fundamental understanding on this process is still required for the design of novel materials with the complexity of nature. Here, we utilized single-molecule force spectroscopy to elucidate the mechanism of interaction between mica and a mica-binding peptide. The mica-binding peptide was selected from previously reported phage display study. Using alanine scan we gained information on the importance of each amino acid in the peptide sequence for mica binding. Our studies revealed the importance of the amino acid proline for this interaction. Moreover, molecular dynamic simulations demonstrated the importance of the conformational freedom of the peptide. These results shade light on the interaction between peptides and inorganic materials and of great significance for the design of new composite materials.