Molecular structures of peptides and proteins chemically immobilized on SAM and polymer surfaces were deduced using sum frequency generation (SFG) vibrational spectroscopy and attenuated total reflectance (ATR) � FTIR. A variety of peptides including cecropin P1, MSI-78, tachyplesin I, and FSD-1 were investigated. It was found that both the peptide surface immobilization site and the surface coverage affect the conformation and orientation of surface immobilized peptides. The different orientation and conformation also led to different activities. Two enzyme molecules, 6-phospho-�-galactosidase (�-Gal) and nitroreductase (NsfB) were examined using SFG and ATR-FTIR. The enzymes were immobilized onto the surface via specific cysteine sites and the orientations were detected using SFG and ATR-FTIR. This research demonstrated the feasibility to control the surface immobilized enzyme orientation, and showed that enzymes with the optimized orientation enhance the activity.

Structure and activity of chemically immobilized peptides and proteins on surfaces

247th National Meeting (2014)

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