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Title: Antimicrobial properties of analgesic kyotorphin peptides unraveled through atomic force microscopy
Author: Ribeiro, Marta M. B.
Franquelim, Henri G.
Torcato, Inês M.
Ramu, Vasanthakumar G.
Heras, Montserrat
Bardaji, Eduard R.
Castanho, Miguel A. R. B.
Keywords: Kyotorphin derivatives
Atomic force microscopy
Issue Date: 2012
Publisher: Elsevier
Citation: Biochemical and Biophysical Research Communications 420 (2012) 676–679
Abstract: Antimicrobial peptides (AMPs) are promising candidates as alternatives to conventional antibiotics for the treatment of resistant pathogens. In the last decades, new AMPs have been found from the cleavage of intact proteins with no antibacterial activity themselves. Bovine hemoglobin hydrolysis, for instance, results in AMPs and the minimal antimicrobial peptide sequence was defined as Tyr-Arg plus a positively charged amino acid residue. The Tyr-Arg dipeptide alone, known as kyotorphin (KTP), is an endogenous analgesic neuropeptide but has no antimicrobial activity itself. In previous studies new KTP derivatives combining C-terminal amidation and Ibuprofen (Ib) – KTP–NH2, IbKTP, IbKTP–NH2 – were designed in order to improve KTP brain targeting. Those modifications succeeded in enhancing peptide-cell membrane affinity towards fluid anionic lipids and higher analgesic activity after systemic injection resulted therefrom. Here, we investigated if this affinity for anionic lipid membranes also translates into antimicrobial activity because bacteria have anionic membranes. Atomic force microscopy revealed that KTP derivatives perturbed Staphylococcus aureus membrane structure by inducing membrane blebbing, disruption and lysis. In addition, these peptides bind to red blood cells but are non-hemolytic. From the KTP derivatives tested, amidated KTP proves to be the most active antibacterial agent. The combination of analgesia and antibacterial activities with absence of toxicity is highly appealing from the clinical point of view and broadens the therapeutic potential and application of kyotorphin peptides.
Description: © 2012 Elsevier Inc. All rights reserved
Peer review: yes
ISSN: 0006-291X
Appears in Collections:IMM - Artigos em Revistas Internacionais

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