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Stepwise self-assembly of a tripeptide from molecular dimers to supramolecular beta-sheets in crystals and amyloid-like fibrils in the solid state

Das, A.K., Banerjee, A., Drew, M.G.B., Haldar, D. and Banerjee, A. (2004) Stepwise self-assembly of a tripeptide from molecular dimers to supramolecular beta-sheets in crystals and amyloid-like fibrils in the solid state. Supramolecular Chemistry, 16 (5). pp. 331-335. ISSN 1061-0278

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To link to this item DOI: 10.1080/1061027042000213047

Abstract/Summary

The terminally protected tripeptide Boc-Ala(1)-Leu(2)-Ala(3)-OMe 1 forms antiparallel hydrogen-bonded dimers of two different conformers in the asymmetric unit and the individual dimers then self-associate to form supramolecular beta-sheet structures in crystals and amyloid-like fibrils in the solid state.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11172
Uncontrolled Keywords:self-assembly, molecular dimer, pepticle, amyloid-like fibrils , HYDROGEN-BONDED DIMERS, UNNATURAL AMINO-ACID, CRYSTALLOGRAPHIC SIGNATURE, ALZHEIMERS-DISEASE, PROTEIN, PEPTIDES, FIBRILLOGENESIS, AGGREGATION, OLIGOMERS, COMPLEXES

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