Vibrational spectroscopic studies on fibrinogen adsorption at polystyrene/protein solution interfaces: hydrophobic side chain and secondary structure changes.
Structural changes of fibrinogen after adsorption to polystyrene (PS) were examined at the PS/protein solution interface in situ using sum frequency generation (SFG) vibrational spectroscopy and attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Different behaviors of hydrophobic side chains and secondary structures of adsorbed fibrinogen molecules have been observed. Our results indicate that upon adsorption, the hydrophobic PS surface induces fast structural changes of fibrinogen molecules by aligning some hydrophobic side chains in fibrinogen so that they face to the surface. Such structural changes of fibrinogen hydrophobic side chains are local changes and do not immediately induce significant changes of the protein secondary structures. Our research also shows that the interactions between adsorbed fibrinogen and the PS surface can induce significant changes of protein secondary structures or global conformations which occur on a much longer time scale.
Wang
Jie
J
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
Chen
Xiaoyun
X
Clarke
Matthew L
ML
Chen
Zhan
Z
D000327:Adsorption; D005340:Fibrinogen / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D011137:Polystyrenes / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis; D013499:Surface Properties; D014732:Vibration
D011137:Polystyrenes; D012996:Solutions; D005340:Fibrinogen