Conventional antibiotics might fail in the treatment of biofilm-associated infections causing infection recurrence and chronicity. The search for antimicrobial peptides has been performed with the aim to discover novel anti-infective agents active on pathogens in both planktonic and biofilm associated forms. The fragment 9–19 of human thymosin b4 was studied through 1 ls MD simulation.Two main conformations of the peptide were detected, both constituted by a central hydrophobic core and by the presence of peripheral charged residues suggesting a possible mechanism of interaction with two models of biological membranes, related to eukaryotic or bacterialmembrane respectively. In addition, the peptide was chemically synthesized and its antimicrobial activity was tested in vitro against planktonic and biofilm form of a group of reference strains of Staphylococcus spp. and oneP. aeruginosa strain. The human thymosin b4 fragment EIEKFDKSKLK showed antibacterial activity against staphylococcal strains and Pseudomonas aeruginosaATCC 15442 at concentrations from 12.5 to 6.2 mg/ml andinhibited biofilm formation at sub-inhibitory concentrations (3.1–0.75 mg/ml). The activity of the fragment in inhibitingbiofilm formation, could be due to the conformations highlighted by the MD simulations, suggesting its interaction with the bacterial membrane. Human thymosin b4 fragment can be considered a promising lead compound todevelop novel synthetic or recombinant derivatives withimproved pharmaceutical potential.
|Numero di pagine||9|
|Rivista||WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY|
|Stato di pubblicazione||Published - 2016|