Dipeptide Nanotubes, with N-Terminally Located ω-Amino Acid Residues, That are Stable Proteolytically, Thermally, and Over a Wide Range of pH
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Dipeptide Nanotubes, with N-Terminally Located ω-Amino Acid
Residues, That are Stable Proteolytically, Thermally, and Over a
Wide Range of pH
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| Creator |
Guha, Samit
Drew, Michael G. B Banerjee, Arindam |
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| Subject |
Chemistry
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| Description |
Two dipeptides containing an N-terminally positioned ω-amino acid residue (�-alanine/δ-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 ω-amino acid residues and C-terminally positioned
R-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.
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| Date |
2008
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/277/1/CHEMISTRY_OF_MATERIALS%2C__20(_6)%2C_2282%2D2290%2C2008[110].pdf
Guha, Samit and Drew, Michael G. B and Banerjee, Arindam (2008) Dipeptide Nanotubes, with N-Terminally Located ω-Amino Acid Residues, That are Stable Proteolytically, Thermally, and Over a Wide Range of pH. Chem. Mater, 20 (6). pp. 2282-2290. |
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| Relation |
http://dx.doi.org/10.1021/cm703159b
http://www.eprints.iicb.res.in/277/ |
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