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Biochim Biophys Acta. 2013 Jun;1830(6):3767-75. doi: 10.1016/j.bbagen.2013.01.026. Epub 2013 Feb 9.

Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria.

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1
Università di Napoli Federico II, Dipartimento delle Scienze Biologiche, Napoli, Italy.

Abstract

BACKGROUND:

Temporins are small antimicrobial peptides secreted by the Rana temporaria showing mainly activity against Gram-positive bacteria. However, different members of the temporin family, such as Temporin B, act in synergy also against Gram-negative bacteria. With the aim to develop a peptide with a wide spectrum of antimicrobial activity we designed and analyzed a series of Temporin B analogs.

METHODS:

Peptides were initially obtained by Ala scanning on Temporin B sequence; antimicrobial activity tests allowed to identify the TB_G6A sequence, which was further optimized by increasing the peptide positive charge (TB_KKG6A). Interactions of this active peptide with the LPS of E. coli were investigated by CD, fluorescence and NMR.

RESULTS:

TB_KKG6A is active against Gram-positive and Gram-negative bacteria at low concentrations. The peptide strongly interacts with the LPS of Gram-negative bacteria and folds upon interaction into a kinked helix.

CONCLUSION:

Our results show that it is possible to widen the activity spectrum of an antimicrobial peptide by subtle changes of the primary structure. TB_KKG6A, having a simple composition, a broad spectrum of antimicrobial activity and a very low hemolytic activity, is a promising candidate for the design of novel antimicrobial peptides.

GENERAL SIGNIFICANCE:

The activity of antimicrobial peptides is strongly related to the ability of the peptide to interact and break the bacterial membrane. Our studies on TB_KKG6A indicate that efficient interactions with LPS can be achieved when the peptide is not perfectly amphipathic, since this feature seems to help the toroidal pore formation process.

PMID:
23403136
DOI:
10.1016/j.bbagen.2013.01.026
[Indexed for MEDLINE]
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