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The role of terminal tyrosine residues in the formation of tripeptide nanotubes: a crystallographic insight

Ray, S., Drew, M.G.B., Das, A.K. and Banerjee, A. (2006) The role of terminal tyrosine residues in the formation of tripeptide nanotubes: a crystallographic insight. Tetrahedron, 62 (31). pp. 7274-7283. ISSN 0040-4020

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To link to this item DOI: 10.1016/j.tet.2006.05.042

Abstract/Summary

Terminally protected acyclic tripeptides containing tyrosine residues at both termini self-assemble into nanotubes in crystals through various non-covalent interactions including intermolecular hydrogen bonds. The nanotube has an average internal diameter of 5 angstrom (0.5 nm) and the tubular ensemble is developed through the hydrogen-bonded phenolic-OH side chains of tyrosine (Tyr) residues [Org. Lett. 2004, 6, 4463]. We have synthesized and studied several tripeptides 3-6 to probe the role of tyrosine residues in nanotube structure formation. These peptides either have only one Tyr residue at N- or C-termini or they have one or two terminally located phenylalanine (Phe) residues. These tripeptides failed to form any kind of nanotubular structure in the solid state. Single crystal X-ray diffraction studies of these peptides 3-6 clearly demonstrate that substitution of any one of the terminal Tyr residues in the Boc-Tyr-X-Tyr-OMe (X=VaI or Ile) sequence disrupts the formation of the nanotubular structure indicating that the presence of two terminally located Tyr residues is vital for nanotube formation. (c) 2006 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11580
Uncontrolled Keywords:acyclic peptides, tyrosine, nanotube, self-assembly, ASSEMBLING ORGANIC NANOTUBES, HELICAL ROSETTE NANOTUBES, PEPTIDE, NANOTUBES, ION CHANNELS, DIFFRACTION DATA, CYCLIC-PEPTIDES, AMINO-ACID, CONFORMATION, ARCHITECTURE, TRANSPORT

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