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
Peptidesjournal_title
Peptidesauthors
Varkey J,Singh S,Nagaraj Rdoi
10.1016/j.peptides.2006.06.010subject
Has Abstractpub_date
2006-11-01 00:00:00pages
2614-23issue
11eissn
0196-9781issn
1873-5169pii
S0196-9781(06)00310-Xjournal_volume
27pub_type
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