TY - JOUR
TI - Hierarchical self-assembly in diblock copolypeptides of poly(γ-benzyl-l-glutamate) with poly poly(l-leucine) and poly(O-benzyl-l-tyrosine)
AU - M. Mondeshki
AU - H.W. Spiess
AU - T. Aliferis
AU - H. Iatrou
AU - N. Hadjichristidis
AU - G. Floudas
JO - European Polymer Journal
PY - 2011
VL - 47
TODO - 4
SP - 668--674
PB - ELSEVIER BV
SN - 0014-3057
TODO - 10.1016/j.eurpolymj.2010.10.011
TODO - Block copolypeptides;  Copolypeptides;  Diblocks;  Hierarchical self-assembly;  L-glutamate;  L-leucine;  l-Tyrosine;  Nano scale;  Nanometer length scale;  Peptide secondary structures;  Secondary structures, Phase separation;  Polypeptides;  Self assembly, Amino acids
TODO - Block copolypeptides with their inherent nanometer length scale of phase separation, provide means of manipulating the type (α-helices, β-strands) and persistence of peptide secondary structures. Two such examples are employed based on the α-helical poly(γ-benzyl-l- glutamate) (PBLG) polypeptide as one block and poly(l-leucine) (α-helical) or poly(O-benzyl-l-tyrosine) (POBT) (β-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 β-sheets and to maintain the defected α-helices of PBLG and PLEU with a limited lateral coherence. © 2010 Elsevier Ltd. All rights reserved.
ER -