@article{2959215,
    title = "Hierarchical self-assembly in diblock copolypeptides of poly(γ-benzyl-l-glutamate) with poly poly(l-leucine) and poly(O-benzyl-l-tyrosine)",
    author = "M. Mondeshki and H.W. Spiess and T. Aliferis and H. Iatrou and N. Hadjichristidis and G. Floudas",
    journal = "European Polymer Journal",
    year = "2011",
    volume = "47",
    number = "4",
    pages = "668--674",
    publisher = "ELSEVIER BV",
    issn = "0014-3057",
    doi = "10.1016/j.eurpolymj.2010.10.011",
    keywords = "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",
    abstract = "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."
}