Sitaram, Narasimhaiah ; Sai, Korrapati Purna ; Singh, Shashi ; Sankaran, Krishnan ; Nagaraj, Ramakrishnan (2002) Structure-function relationship studies on the frog skin antimicrobial peptide tigerinin 1: design of analogs with improved activity and their action on clinical bacterial isolates Antimicrobial Agents and Chemotherapy, 46 (7). pp. 2279-2283. ISSN 0066-4804
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Official URL: http://aac.asm.org/cgi/content/abstract/46/7/2279
Related URL: http://dx.doi.org/10.1128/AAC.46.7.2279-2283.2002
Abstract
Structure-function relationships in antimicrobial peptides have been extensively investigated in order to obtain improved analogs. Most of these studies have targeted either α-helical peptides or β-sheet peptides with multiple disulfide bridges. Tigerinins are short, nonhelical antimicrobial peptides with a single disulfide bridge. In this study, we have synthesized several analogs of tigerinin 1 with an aim to understand the structural basis of activity as well as improve its activity. The studies demonstrate that the loop structure of tigerinin 1 is essential for its optimal activity. However, linearization with increased cationic charges can compensate for loss of loop structure to some extent. Morphology of the cells after treatment with the active analogs shows extensive leakage of cytoplasmic contents. Tigerinin 1 and two of its analogs exhibit impressive activity against a variety of clinical bacterial isolates.
Item Type: | Article |
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Source: | Copyright of this article belongs to American Society for Microbiology. |
ID Code: | 23991 |
Deposited On: | 01 Dec 2010 12:48 |
Last Modified: | 17 May 2016 07:46 |
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