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Dipeptide nanotubes, with n-terminally located omega-amino acid residues, that are stable proteolytically, thermally, and over a wide range of pH

Guha, S., Drew, M. G. B. and Banerjee, A. (2008) Dipeptide nanotubes, with n-terminally located omega-amino acid residues, that are stable proteolytically, thermally, and over a wide range of pH. Chemistry of Materials, 20 (6). pp. 2282-2290. ISSN 0897-4756

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To link to this item DOI: 10.1021/cm703159b

Abstract/Summary

Two dipeptides containing an N-terminally positioned omega-amino acid residue (beta-alanine/delta-amino valeric acid) self-assembles to form nanotubes in the solid state as well as in aqueous solution. In spite of having hollow nanotubular structures in the solid state and in solution, their self-assembling nature in these two states are different and this leads to the formation of different internal diameters of these nanotubes in solution and in solid state structure. These nanotubes are stable proteolytically, thermally, and over a wide range of pH values (1-13). The role of water molecules in nanotube formation has been investigated in the solid state. These nanotubes can be considered as a new class of dipeptide nanotubes as they are consisting of N-terminally located protease resistant omega-amino acid residues and C-terminally positioned alpha-amino acid residues. These dipeptides can form an interesting class of short peptidic structure that can give rise to stable nanotubular structure upon self-assembly and these nanotubes can be explored in future for potential nanotechnological applications.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11293
Uncontrolled Keywords:PEPTIDE NANOTUBES, HYDROPHOBIC DIPEPTIDES, AMYLOID POLYPEPTIDE, HAIRPIN, PEPTIDE, CRYSTAL, DESIGN, NANOSTRUCTURES, OLIGOPEPTIDES, RECOGNITION, NANOWIRES

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