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Supramolecular peptide helix from a novel double turn forming peptide containing a β-amino acid

✍ Scribed by Arijit Banerjee; Samir Kumar Maji; Michael G.B. Drew; Debasish Haldar; Arindam Banerjee

Book ID
104252768
Publisher
Elsevier Science
Year
2003
Tongue
French
Weight
163 KB
Volume
44
Category
Article
ISSN
0040-4039

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✦ Synopsis

A single-crystal X-ray diffraction study of the terminally protected tetrapeptide Boc-b-Ala-Aib-Leu-Aib-OMe 1 (Aib: a-aminoisobutyric acid; b-Ala: b-Alanine) reveals that it adopts a new type of double turn structure which self-associates to form a unique supramolecular helix through intermolecular hydrogen bonds. Scanning electron microscopic studies show that peptide 1 exhibits amyloid-like fibrillar morphology in the solid state.

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## Abstract The increasing interest in click chemistry and its use to stabilize turn structures led us to compare the propensity for β‐turn stabilization of different analogs designed as mimics of the β‐turn structure found in tendamistat. The β‐turn conformation of linear β‐amino acid‐containing p