Estudo teórico-computacional sobre a flexibilidade conformacional do peptídeo antimicrobiano Latarcin-2a

Abstract

It is common ground in the literature that the antimicrobial peptide Latarcin-2a, extracted from the venom of the spider Lachesana tarabaevi, performs its activity because of its stable alphahelix structure. The biological evolution of macromolecules of this type, however, point to the development of the ability to adapt to the environment in which it is inserted, conferring relevant characteristics with respect to both structure and activity. Our work shows by means of molecular dynamics techniques and tools that the peptide Latarcin-2a, different from what was believed, is an intrinsically disordered peptide, endowed with functional plasticity derived from its conformational flexibility.