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Can a consecutive double turn conformation be considered as a peptide based molecular scaffold for supramolecular helix in the solid state?

Das, A.K., Banerjee, A., Drew, M.G.B., Ray, S. and Haldar, D. (2005) Can a consecutive double turn conformation be considered as a peptide based molecular scaffold for supramolecular helix in the solid state? Tetrahedron, 61 (21). pp. 5027-5036. ISSN 0040-4020

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To link to this item DOI: 10.1016/j.tet.2005.03.057

Abstract/Summary

Helices and sheets are ubiquitous in nature. However, there are also some examples of self-assembling molecules forming supramolecular helices and sheets in unnatural systems. Unlike supramolecular sheets there are a very few examples of peptide sub-units that can be used to construct supramolecular helical architectures using the backbone hydrogen bonding functionalities of peptides. In this report we describe the design and synthesis of two single turn/bend forming peptides (Boc-Phe-Aib-Ile-OMe 1 and Boc-Ala-Leu-Aib-OMe 2) (Aib: alpha-aminoisobutyric acid) and a series of double-turn forming peptides (Boc-Phe-Aib-IIe-Aib-OMe 3, Boc-Leu-Aib-Gly-Aib-OMe 4 and Boc-gamma-Abu-Aib-Leu-Aib-OMe 5) (gamma-Abu: gamma-aminobutyric acid). It has been found that, in crystals, on self-assembly, single turn/bend forming peptides form either a supramolecular sheet (peptide 1) or a supramolecular helix (peptide 2). unlike self-associating double turn forming peptides, which have only the option of forming supramolecular helical assemblages. (c) 2005 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11173
Uncontrolled Keywords:Aib, double turn conformation, 'S' shaped molecular structure, supramolecular helix, 1ST CRYSTALLOGRAPHIC SIGNATURE, ALPHA-HELIX, WATER-MOLECULES, AMINO-ACIDS, BETA-SHEETS, SINGLE, DESIGN, OLIGOPEPTIDES, TETRAPEPTIDE, RECOGNITION

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