A new motif in the formation of peptide nanotubes: the crystallographic signature.
Terminally protected acyclic tripeptides Boc-Tyr(1)-Val(2)-Tyr(3)-OMe 1 and Boc-Tyr(1)-Ile(2)-Tyr(3)-OMe 2 self-assemble into nanotubes in crystals through various noncovalent interactions with an average internal diameter of 5 A (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. [structure: see text]
Ray
Sudipta
S
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700 032, India.
Haldar
Debasish
D
Drew
Michael G B
MG
Banerjee
Arindam
A
D003460:Crystallization; D006860:Hydrogen Bonding; D043942:Nanotubes / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D014443:Tyrosine / Q000737:chemistry
D009842:Oligopeptides; D014443:Tyrosine