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 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.