http://www.cnr.it/ontology/cnr/individuo/prodotto/ID208613
Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria (Articolo in rivista)
- Type
- Label
- Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbagen.2013.01.026 (literal)
- Alternative label
Avitabile C, Netti F, Orefice G, Palmieri M, Nocerino N, Malgieri G, D'Andrea LD, Capparelli R, Fattorusso R, Romanelli A. (2013)
Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria
in Biochimica et biophysica acta. G, General subjects (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Avitabile C, Netti F, Orefice G, Palmieri M, Nocerino N, Malgieri G, D'Andrea LD, Capparelli R, Fattorusso R, Romanelli A. (literal)
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- ISI Web of Science (WOS) (literal)
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- Università di Napoli \"Federico II\"
Istituto di Biostrutture e Bioimmagini, CNR
Seconda Università di Napoli (literal)
- Titolo
- Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria (literal)
- 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. (literal)
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