Perturbation of long-range water dynamics as the mechanism for the antifreeze activity of antifreeze glycoprotein.

ABSTRACT: Very little is known about the mechanism of antifreeze action of antifreeze glycoproteins (AFGPs) present in Antarctic teleost fish. Recent NMR and CD studies assisted with total synthesis of synthetic AFGP variants have provided insight into the structure of short AFGP glycopeptides, though the observations did not yield information on the antifreeze mechanism of action. In this study, we use Hamiltonian replica exchange (HREX) molecular dynamics simulations to probe the structure and surrounding aqueous environments of both the natural (AFGP8) and synthetic (s-AFGP4) AFGPs. AFGPs can adopt both amphiphilic and pseudoamphiphilic conformations, the preference of which is related to the proline content of the peptide. The arrangement of carbohydrates allows the hydroxyl groups on terminal g

SUBMITTER: Mallajosyula SS 

PROVIDER: S-EPMC4191590 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature