Journalartikel

Enhanced antifungal and insect α-amylase inhibitory activities of Alpha-TvD1, a peptide variant of Tephrosia villosa defensin (TvD1) generated through in vitro mutagenesis


AutorenlisteVijayan, S; Imani, J; Tanneeru, K; Guruprasad, L; Kogel, KH; Kirti, PB

Jahr der Veröffentlichung2012

Seiten220-229

ZeitschriftPeptides

Bandnummer33

Heftnummer2

ISSN0196-9781

DOI Linkhttps://doi.org/10.1016/j.peptides.2011.12.020

VerlagElsevier


Abstract

TvD1 is a small, cationic, and highly stable defensin from the weedy legume, Tephrosia villosa with demonstrated in vitro antifungal activity. We show here peptide modifications in TvD1 that lead to enhanced antifungal activities. Three peptide variants, S32R, D37R, and Alpha-TvD1 (-G-M-T-R-T-) with variations in and around the beta 2-beta 3 loop region that imposes the two beta-strands, beta 2 and beta 3 were generated through in vitro mutagenesis. Alpha-TvD1 exhibited enhanced antifungal activity against the fungal pathogens. Fusarium culmorum and Fusarium oxysporum with respective IC50 values of 2.5 mu M and 3.0 mu M, when compared to S32R (<5.0 mu M and >5.0 mu M), D37R (5.5 mu M and 4.5 mu M), and the wild type TvD1 (6.5 mu M). Because of the enhanced antifungal activity, this variant peptide was characterized further. Growth of F. culmorum in the presence of Alpha-TvD1 showed deformities in hyphal walls and nuclear damage. With respect to the plant pathogenic bacterium. Pseudomonas syringae pv. tomato strain DC3000, both Alpha-TvD1 and the wild type TvD1 showed comparable antibacterial activity. Both wild type TvD1 and Alpha-TvD1 displayed inhibitory activity against the alpha-amylase of the mealworm beetle, Tenebrio molitor (TMA) with the latter showing enhanced activity. The human salivary as well as barley alpha-amylase activities were not inhibited even at concentrations of up to 50 mu M, which has been predicted to be due to differences in the pocket size and the size of the interacting loops. Present study shows that the variant Alpha-TvD1 exhibits enhanced antifungal as well as insect alpha-amylase inhibitory activity.




Autoren/Herausgeber




Zitierstile

Harvard-ZitierstilVijayan, S., Imani, J., Tanneeru, K., Guruprasad, L., Kogel, K. and Kirti, P. (2012) Enhanced antifungal and insect α-amylase inhibitory activities of Alpha-TvD1, a peptide variant of Tephrosia villosa defensin (TvD1) generated through in vitro mutagenesis, Peptides, 33(2), pp. 220-229. https://doi.org/10.1016/j.peptides.2011.12.020

APA-ZitierstilVijayan, S., Imani, J., Tanneeru, K., Guruprasad, L., Kogel, K., & Kirti, P. (2012). Enhanced antifungal and insect α-amylase inhibitory activities of Alpha-TvD1, a peptide variant of Tephrosia villosa defensin (TvD1) generated through in vitro mutagenesis. Peptides. 33(2), 220-229. https://doi.org/10.1016/j.peptides.2011.12.020



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