Conformational Study on Membrane-Promoting  α -HelixFormation of Dynorphin-A (1–17) Using the Wang-Landau Method

Abstract

ABSTRACT: Dynorphin-A (1–17) and its variant, R6W-DNYA, are known to penetrate into the plasma membrane and to cause lysis and fusion. Peptide-membrane interactions promote  α -helix formations of these peptides. To investigate the membrane-promoting  α -helix formation, we systematically compute low-energy  α -helical conformations using the Wang- Landau method, and evaluate their solvation free-energies in cyclohexane solvent corresponding to the hydrophobic environment of a membrane. The result suggests that Dynorphin-A (1–17) and R6W-DNYA existing in a membrane may form  α -helices in two regions of Gly³-Ile⁸ and Leu¹²-Gln¹⁷.