RESUMO
A new fluorescent peptide probe for the detection of Zn(2+) was synthesized on the basis of zinc binding ligands in zinc enzymes. The peptide that has a unique amino acid sequence displayed a great selectivity for Zn(2+) in the presence of several transition metal ions in aqueous solution. The reversibility, binding stoichiometry, binding affinity, and pH sensitivity of the sensor were studied. Further, on-bead application of the peptide as chemosensors was demonstrated.
Assuntos
Desenho de Fármacos , Corantes Fluorescentes/síntese química , Peptídeos/síntese química , Soluções/análise , Água/análise , Zinco/análise , Avaliação Pré-Clínica de Medicamentos/métodos , Corantes Fluorescentes/análise , Peptídeos/análise , Soluções/química , Água/química , Zinco/químicaRESUMO
We synthesized a novel peptide-resin conjugate by immobilizing beta-sheet antibacterial peptide on PEG-PS resin. The peptide-resin conjugate, similar to cationic antimicrobial peptides, demonstrated unique properties such as potent antibacterial activity, no hemolytic activity, lipid membrane perturbation activity, and potent synergism with vancomycin. Specially, the peptide-resin conjugate showed a more increased lipid membrane perturbation activity in comparison to unbound beta-sheet antibacterial peptide.
