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Conformational studies of multichain copoly(α-amino acids)s in solution

  • Colloid Science
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Abstract

The conformational transition of multichain copoly(α-amino acid)s consisting of copoly(γ-methyl-L-glutamyl-L-lysine) as backbone molecule and poly(γ-benzyl-L-glutamate) as branch molecules was studied in chloroform and DCA mixtures. The helix stability of backbone molecule is strongly affected by the length of branch molecules. In the case of the multichain copolymer having short branch molecular chains, i.e.,DP br <10, the helix conformation of the backbone molecule is strictly affected by some interferences among the randomly coiled molecular chains. In the case of water-soluble multichain copolymer having poly(L-glutamic acid) or poly(L-lysine) as branch molecules, the transitional process from coil to helix is observed by depressing hydrostatic repulsion among the ionized side chain of branch molecules. However, such conformational transition is depressed to a considerable extent by interferences among the branch molecules.

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Abbreviations

A/I :

molar ratio of NCA to initiator

Cbz:

carbobenzyloxy

DCA:

dichloroacetic acid

DMF:

N,N-dimethylformamide

DP br :

number-average degree of polymerization of branches of multichain copolymer

Fw br :

weight fraction ofγ-benzyl-L-glutamyl residues of multichain copolymer

Mn :

number-average molecular weight

NCA:

N-carboxy anhydride ofα-amino acid

ORD:

optical rotatory dispersion

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Sakamoto, M., Kuroyanagi, Y. Conformational studies of multichain copoly(α-amino acids)s in solution. Colloid & Polymer Sci 262, 418–422 (1984). https://doi.org/10.1007/BF01410262

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  • DOI: https://doi.org/10.1007/BF01410262

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