Abstract
Block copolypeptides with their inherent nanometer length scale of phase separation, provide means of manipulating the type (alpha-helices, beta-strands) and persistence of peptide secondary structures. Two such examples are employed based on the alpha-helical poly(gamma-benzyl-L-glutamate) (PBLG) polypeptide as one block and poly(L-leucine) (alpha-helical) or poly(O-benzyl-L-tyrosine) (POBT) (beta-strands) as the second block. Although both secondary structures are present in the copolypeptides the effect of nano-scale confinement is to induce folding in the POBT beta-sheets and to maintain the defected alpha-helices of PBLG and PLEU with a limited lateral coherence. (C) 2010 Elsevier Ltd. All rights reserved.