Sudha, T. S. ; Balaram, P. (1983) Stabilization of β-turn conformations in enkephalins α-Aminoisobutyric acid analogs International Journal of Peptide and Protein Research, 21 (4). pp. 381-388. ISSN 0367-8377
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Official URL: http://www3.interscience.wiley.com/journal/1215297...
Related URL: http://dx.doi.org/10.1111/j.1399-3011.1983.tb03119.x
Abstract
Stereochemical constraints have been introduced into the enkephalin backbone by substituting α-aminoisobutyryl (Aib) residues at positions 2 and 3, instead of Gly. 1H n.m.r. studies of Tyr-Aib-Gly-Phe-Met-NH2, Tyr-Aib-Aib-Phe-Met-NH2 and Tyr-Gly-Aib-Phe-Met-NH2 demonstrate the occurrence of folded, intramolecularly hydrogen bonded structures in organic solvents. Similar conformations are also favoured in the corresponding t-butyloxycarbonyl protected tetrapeptides, which lack the Tyr residue. A β-turn centred at positions 2 and 3 is proposed for the Aib2-Gly3 analog. In the Gly2-Aib3 analog, the β-turn has Aib3-Phe4 as the corner residues. The Aib2-Aib3 analog adopts a consecutive β-turn or 310 helical conformation. High in vivo biological activity is observed for the Aib2 and Aib2-Aib3 analogs, while the Aib3 peptide is significantly less active.
Item Type: | Article |
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Source: | Copyright of this article belongs to Munksgaard International Publishers. |
Keywords: | α-aminoisobutyryl Peptides; Enkephalin Analogs; Conformational Constraints; Peptide Conformation; β-turns |
ID Code: | 4516 |
Deposited On: | 18 Oct 2010 07:37 |
Last Modified: | 16 May 2016 15:09 |
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