The performance of a biosensor using immobilized peptides or proteins as biological recognition elements depends on the conformation and orientation of such peptides and proteins. We successfully applied sum frequency generation (SFG) vibrational spectroscopy, supplemented by attenuated total reflectance (ATR)-Fourier transform infrared spectroscopy to determine conformations and orientations of various peptides and proteins immobilized on surfaces. Various surfaces such as self-assembled monolayers and polymers have been used in the study. Peptides immobilized via different positions, e.g., N-terminal amino acid, C-terminal amino acid, as well as amino acids in the middle, have been investigated. Conformations and orientations of immobilized peptides and proteins were successfully deduced in dry air, in water, and in humid air with different humidity levels. Such orientations and conformations were well correlated to the functions of these immobilized peptides and proteins.

Molecular structures of peptides and proteins chemically immobilized on surfaces

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.