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A new motif in the formation of peptide nanotubes: the crystallographic signature

Ray, S., Haldar, D., Drew, M.G.B. and Banerjee, A. (2004) A new motif in the formation of peptide nanotubes: the crystallographic signature. Organic Letters, 6 (24). pp. 4463-4465. ISSN 1523-7060

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To link to this item DOI: 10.1021/ol048253a

Abstract/Summary

Terminally protected acyclic tripeptides Boc-Tyr(1)-Val(2)-Tyr(3)-OMe 1 and Boc-Tyr(1)-lle(2)-Tyr(3)-OMe 2 self-assemble into nanotubes in crystals through various noncovalent interactions with an average internal diameter of 5 Angstrom (0.5 nm), and the tubular ensemble is developed through the hydrogen-bonded side chains of tyrosine residues. The inside of the hollow nanotubular structures is hydrophilic; however, no solvent molecules have been crystallographically detected.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11583
Uncontrolled Keywords:ASSEMBLING ORGANIC NANOTUBES, HELICAL ROSETTE NANOTUBES, CYCLIC-PEPTIDES, DESIGN

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