Design of a new foldamer turn-linker-turn in acyclic hexapeptides and formation of channels through self-assemblyDutta, 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 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1016/j.molstruc.2008.07.001 Abstract/SummarySingle 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.
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