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Overlapping double turn conformations adopted by tetrapeptides containing non-coded α-amino isobutyric acid (AIB) and formation of tape-like structures through supramolecular helix mediated self- assembly
S KAR, A DUTTA, M G B DREW, P KOLEY,
Published in -
2009
PMID: 19508219
Volume: 16
   
Issue: 9
Pages: 1063 - 1073
Abstract
Single crystal X-ray diffraction studies and solvent dependent 1H NMR titrations reveal that a set of four tetrapeptides with general formula Boc-Xx(1)-Aib(2)-Yy(3)-Zz(4)-OMe, where Xx, Yy and Zz are coded L-amino acids, adopt equivalent conformations that can be described as overlapping double turn conformations stabilized by two 4→1 intramolecular hydrogen bonds between Yy(3)-NH and Boc C=O and Zz(4)-NH and Xx(1)C=O. In the crystalline state, the double turn structures are packed in head-to-tail fashion through intermolecular hydrogen bonds to create supramolecular helical structures. Field emission scanning electron microscopic (FE-SEM) images of the tetrapeptides in the solid state reveal that they can form flat tape-like structures. The results establish that synthetic Aib containing supramolecular helices can form highly ordered self-aggregated amyloid plaque like human amylin. © 2009 Bentham Science Publishers Ltd.
About the journal
JournalProtein and Peptide Letters
Publisher-
ISSN0929-8665
Open AccessNo