Antibacterial activity of linear peptides spanning the carboxy-terminal beta-sheet domain of arthropod defensins.

Abstract:

:The antibacterial activity of peptides without disulfide bridges, spanning the carboxy-terminal segment of arthropod defensins, has been investigated. Although all the peptides have net positive charges, they exhibited varying antibacterial potencies and spectra. Atomic force and fluorescence microscopic analyses indicate that the peptides exert their activity by permeabilizing the outer and inner membranes of Gram-negative bacteria such as Escherichia coli. It appears that the plasticity observed in the activity of mammalian defensins with respect to sequence, number of disulfide bridges or net positive charge, is also observed in insect defensins.

journal_name

Peptides

journal_title

Peptides

authors

Varkey J,Singh S,Nagaraj R

doi

10.1016/j.peptides.2006.06.010

subject

Has Abstract

pub_date

2006-11-01 00:00:00

pages

2614-23

issue

11

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(06)00310-X

journal_volume

27

pub_type

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