Adsorption of human serum albumin on the chrysotile surface: a molecular dynamics and spectroscopic investigation.

ABSTRACT: The human serum albumin (HSA) secondary structure modifications induced by the chrysotile surface have been investigated via computational molecular dynamics (MD) and experimental infrared spectroscopy (FTIR) on synthetic chrysotile nanocrystals coated with different amount of HSA. MD simulations, conducted by placing various albumin subdomains close to the fixed chrysotile surface, show an initial adsorption phase, accompanied by local rearrangements of the albumin motifs in contact with the chrysotile layer. Next, large-scale rearrangements follow with consequent secondary structure modifications. Gaussian curve fitting of the FTIR spectra obtained for HSA-coated synthetic chrysotile nanocrystals has allowed the quantification of HSA structural modifications as a function of the amount o

SUBMITTER: Artali R 

PROVIDER: S-EPMC2607402 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature