Surface orientation of magainin 2: molecular dynamics simulation and sum frequency generation vibrational spectroscopic studies.

ABSTRACT: We combined molecular dynamics based free energy calculations with sum frequency generation (SFG) spectroscopy to study the orientational distribution of solvated peptides near hydrophobic surfaces. Using a simplified atomistic model of the polystyrene (PS) surface, molecular dynamics simulations have been applied to compute the orientational probability of an α-helical peptide, magainin 2, with respect to the PS/water interface. Free energy calculations revealed that the preferred (horizontal) peptide orientation was driven by the favorable interactions between the hydrophobic PS surface and the hydrophobic residues on the helix, and additional simulations examined the importance of small aggregate formation. Concentration-dependent measurements obtained via SFG vibrational spectroscopy s

SUBMITTER: Boughton AP 

PROVIDER: S-EPMC2953566 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature