6 documents found, page 1 of 1
Temperature‐dependent re‐alignment of the short multifunctional peptide BP100 i...
Strandberg, Erik; Wadhwani, Parvesh; Bürck, Jochen; Anders, Patrick; Mink, Christian; van den Berg, Jonas; Ciriello, Raffaele A. M.; Melo, Manuel N.BP100 is a cationic undecamer peptide with antimicrobial and cell-penetrating activities. The orientation of this amphiphilic α-helix in lipid bilayers was examined under numerous conditions using solid-state 19F, 15N and 2H NMR. At high temperatures in saturated phosphatidylcholine lipids, BP100 lies flat on the membrane surface, as expected. Upon lowering the temperature towards the lipid phase transition, th...
Antifungal and anti-biofilm activity of designed derivatives from kyotorphin
Martins de Andrade, Vitor; Bardají, Eduard; Heras, Montserrat; Ramu, Vasanthakumar G.; Junqueira, Juliana Campos; Diane dos Santos, JéssicaKyotorphin (KTP, l-tyrosyl-l-arginine) is an endogenous analgesic neuropeptide first isolated from bovine brain in 1979. Previous studies have shown that kyotorphins possess anti-inflammatory and antimicrobial activity. Six kyotorphins—KTP-NH2, KTP–NH2–DL, ibuprofen-conjugated KTP (IbKTP), IbKTP-NH2, N-methyl-D-Tyr-L-Arg, and N-methyl-L-Tyr-D-Arg—were designed and synthesized to improve lipophilicity and resist...
Neuropeptide kyotorphin impacts on lipopolysaccharide-induced glucocorticoid-me...
Perazzo, Juliana; Lima, Carla; Heras, Montserrat; Bardají, Eduard; Ferreira, Mônica Lopes; Castanho, Miguel A. R. B.Neuropeptide kyotorphin (KTP) is a potent analgesic if administered directly into the brain. In contrast, KTP-amide (KTP-NH2) is analgesic, neuroprotective, and anti-inflammatory following systemic administration, albeit its mechanism of action is unknown. The aim of this study was to shed light on the mechanism of action of KTP-NH2 at the molecular level. KTP-NH2 does not inhibit the enkephalinases angiotensin...
Escherichia coli cell surface perturbation and disruption induced by antimicrob...
Alves, Carla S.; Melo, Manuel N.; Franquelim, Henri G.; Ferre, Rafael; Planas, Marta; Feliu, Lidia; Bardají, Eduard; Kowalczyk, Wioleta; Andreu, DavidThe potential of antimicrobial peptides (AMPs) as an alter native to conventional therapies is well recognized. Insights into the biological and biophysical properties of AMPs are thus key to understanding their mode of action. In this study, the mech anisms adopted by two AMPs in disrupting the Gram-negative Escherichia coli bacterial envelope were explored. BP100 is a short cecropin A-melittin hybrid peptide ...
Escherichia coli cell surface perturbation and disruption induced by antimicrob...
Alves, Carla S.; Melo, Manuel N.; Franquelim, Henri G.; Ferre, Rafael; Planas, Marta; Feliu, Feliu; Bardají, Eduard; Kowalczyk, Wioleta; Andreu, DavidThe potential of antimicrobial peptides (AMPs) as an alternative to conventional therapies is well recognized. Insights into the biological and biophysical properties of AMPs are thus key to understanding their mode of action. In this study, the mechanisms adopted by two AMPs in disrupting the Gram-negative Escherichia coli bacterial envelope were explored. BP100 is a short cecropin A-melittin hybrid peptide kn...
Synergistic effects of the membrane actions of cecropin-melittin antimicrobial ...
Ferre, Rafael; Melo, Manuel N.; Correia, Ana D.; Feliu, Lidia; Bardají, Eduard; Planas, Marta; Castanho, Miguel A. R. B.BP100 (KKLFKKILKYL-NH2) is a short cecropin A-melittin hybrid peptide, obtained through a combinatorial chemistry approach, which is highly effective in inhibiting both the in vitro and in vivo growth of economically important plant pathogenic Gram-negatives. The intrinsic Tyr fluorescence of BP100 was taken advantage of to study the peptide’s binding affinity and damaging effect on phospholipid bilayers modeli...