Conformational changes of fibrinogen after adsorption.
The adsorption behavior of fibrinogen to two biomedical polyurethanes and a perfluorinated polymer has been investigated. Changes in the secondary structure of adsorbed fibrinogen were monitored using attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) and sum frequency generation vibrational spectroscopy (SFG). SFG measurements were performed in the amide I range as well as in the C-H/N-H stretching range. Amide I signals from SFG demonstrate that fibrinogen has post-adsorption conformational changes that are dependent upon the polymer surface properties. For example, strong attenuation of the amide I and N-H stretching signals with increasing residence time was observed for fibrinogen adsorbed to poly(ether urethane) but not for the other two polymers. This change is not readily observed by ATR-FTIR. Differences in the observed spectral changes for fibrinogen adsorbed to each polymer are explained by different initial binding mechanisms and post-adsorption conformational changes.
Clarke
Matthew L
ML
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
Wang
Jie
J
Chen
Zhan
Z
D000327:Adsorption; D005340:Fibrinogen / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D011487:Protein Conformation; D011791:Quartz; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D013499:Surface Properties; D014732:Vibration
D011108:Polymers; D011791:Quartz; D005340:Fibrinogen