Journal
SUPRAMOLECULAR CHEMISTRY
Volume 21, Issue 8, Pages 681-690Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/10610270802709378
Keywords
peptide; -aminoisobutyric acid; -turn; -sheets; flat morphology
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Funding
- EPSRC
- University of Reading, UK
- CSIR, New Delhi, India
- UGC, New Delhi [32-190/2006]
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Single crystal X-ray diffraction studies show that the three designed tripeptides Boc-Leu-Aib-m-NA-NO2 (I), Boc-Phe-Aib-m-NA-NO2 (II) and Boc-Pro-Aib-m-ABA-OMe (III) (Aib, -aminoisobutyric acid; m-NA, m-nitroaniline; m-ABA, m-aminobenzoic acid; Boc, t-butyloxycarbonyl) containing aromatic rings in the backbones adopt -turn structures that are self-assembled through intermolecular hydrogen bonds and van der Waals interactions to create layers of -sheets. Solvent-dependent NMR titration and CD studies show that the -turn structures of the peptides also exist in the solution phase. The field emission scanning electron microscopic and transmission electron microscopic images of the peptides in the solid state reveal fibrillar structures of flat morphology that are formed through -sheet mediated self-assembly of the preorganised -turn building blocks.
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