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Design of a new foldamer turn-linker-turn in acyclic hexapeptides and formation of channels through self-assembly

Dutta, A., Kar, S., Drew, M. G. B., Koley, P. and Pramanik, A. (2009) Design of a new foldamer turn-linker-turn in acyclic hexapeptides and formation of channels through self-assembly. Journal of Molecular Structure, 917 (2-3). pp. 110-116. ISSN 0022-2860

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To link to this item DOI: 10.1016/j.molstruc.2008.07.001

Abstract/Summary

Single crystal X-ray diffraction studies and solvent dependent NMR titration reveal that the designed pepticles I and 11, Boc-Xx(1)-Aib(2)-Yy(3)-NH(CH2)(2)NH-Yy(3)-Aib(2)-Xx(1)-Boc, where Xx and Yy are lie and Leu in peptide I and Leu and Val in peptide 11, respectively, fold into a turn-linker-turn (T-L-T) conformation both in the solid state and in solution. In the crystalline state the T-L-T foldamers; of peptide I and II self-assemble to form a three-dimensional framework of channels. The insides of the channels are hydrophilic and found to contain solvent CHCl3 hydrogen bonded to exposed C=O of Aib located at the turn regions. (c) 2008 Elsevier B.V. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11239
Uncontrolled Keywords:Peptide, beta-Turn, Foldamer, Self-assembly, Channels, OMEGA-AMINO ACIDS, ALPHA-AMINO, SOLID-STATE, SOLUTION CONFORMATIONS, SECONDARY STRUCTURE, CRYSTAL-STRUCTURES, CORNER RESIDUES, MODEL, PEPTIDES, BETA-PEPTIDES, PROTEINS

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