STUDIES OF THE SURFACE ACTIVITY OF T1CA TEMPORINE IN MEMBRANE MODELS

Antimicrobial Peptides play an important role in the combat of microorganisms, bacteria and fungi.0 Among the several kinds of known peptides, the temporin is particularly notable, that is originally isolated from skins of frogs of the genus Rana temporaria, principally against bacteria. The temporines are short peptides, with strong and fast antibacterial activity, specially against gram-positive and the ESKAPE group. This peptide shows amphipathic structure, which facilitates your interaction with cellular membranes. In this work measurements of surface pressure and tension were taken, to investigate the interaction of a synthetic antimicrobial peptide, similar to the original t1Ca, from the family of temporines, with several membrane models (lipidic monolayers, zwitterionics and negatively charged). The analysis of the insertion of the temporines in this lipidic system were influenced by the surface charge from monolayers, surface pressure and changes in the initial stiffness of the monolayer. Studies of molecular mechanisms of temporines has many interests in pharmacology, because your anti-microorganisms properties have already demonstrated and may corroborate to the development of new infectious diseases approaches, antitumoral therapies, and other things.