Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces.

ABSTRACT: We have characterized the adsorption of bovine fibrinogen onto the biomedical polymer polyethylene terephthalate (PET) by performing mass spectrometric mapping with a lysine-reactive biotin label. After digestion with trypsin, MALDI-TOF mass spectrometry was used to detect peptides from biotinylated bovine fibrinogen, with the goal of identifying lysines that were more accessible for reaction with the chemical label after adsorption. Peptides within domains that are believed to contribute to heparin binding, leukocyte activation, and platelet adhesion were found to be biotin labeled only after bovine fibrinogen adsorbed to the PET surface. Additionally, the accessibility of lysine residues throughout the entire molecule was observed to increase as the concentration of the adsorbing bovine

SUBMITTER: Scott EA 

PROVIDER: S-EPMC2041854 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature