Control of Peptide Secondary Structure and Dynamics in Poly(γ-benzyl-l-glutamate)-b-polyalanine Peptides

• DOI: 10.1021/ma801770b
• Publication Date: 2008-10-16T10:16:41Z
• Authors: A. Gitsas; G. Floudas; M. Mondeshki; H. W. Spiess; T. Aliferis; H. Iatrou; N. Hadjichristidis
• Keywords: Dynamics

The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series poly(γ-benzyl-l-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through combination structural (X-rays, NMR) dynamic (Dielectric Spectroscopy, probes. unfavorable enthalpic interactions between unlike blocks give rise to nanophase separation that results destabilization PAla β-sheets. Contrary this, overall helicity PBLG α-helices is enhanced. "defected" amorphous segments more ordered studied by DS 13C NMR, respectively. These probes provide information on time scale mechanism molecular supramolecular motion.