New Synthetic Peptides Conjugated to Gold Nanoclusters: Antibiotic Activity Against Escherichia coli O157:H7 and Methicillin-Resistant Staphylococcus aureus (MRSA)

Prada Y.A.; Guzmán F.; Ortíz C.; Cabanzo R.; Torres R.; Mejía-Ospino E.

Abstract

Gold nanoclusters protected with bovine serum albumin (AuNC) can be used in multiple biomedical applications through functionalization with two new and bioactive peptides. Both cationic peptides sequences of 17 amino acids in length and the cysteine residue at its C-terminus were designed and synthesized. Peptides were obtained by solid phase synthesis using the Fmoc strategy. Peptides may be coupled via disulfide bonds to AuNC with hydrodynamic size similar to 2 nm +/- 0.3 determined by dynamic light scattering and it had a zeta potential value equal to - 42 mV. Peptides named NBC2253 and NBC2254 were attached to the AuNC using N-succinimidyl-3-(2-pyridyl-dithiol) propionate as crosslinker agent. AuNC@NBC2253 was more active against methicillin-resistant Staphylococcus aureus (MIC50 6.5 mu M) and AuNC@NBC2254 exhibited higher antimicrobial activity than the free peptides on Escherichia coli O157:H7 (MIC50 3.5 mu M). No hemolysis was detected for any of the peptides. It is evidenced that these antimicrobial peptides conjugated to AuNC serve as promising agents to combat some multi-resistant bacterial strains and that the specific binding of these antimicrobial peptides to gold nanoclusters improves the interaction of these nanostructured systems with the biological target.

Más información

Título según WOS: New Synthetic Peptides Conjugated to Gold Nanoclusters: Antibiotic Activity Against Escherichia coli O157:H7 and Methicillin-Resistant Staphylococcus aureus (MRSA)
Título según SCOPUS: New Synthetic Peptides Conjugated to Gold Nanoclusters: Antibiotic Activity Against Escherichia coli O157:H7 and Methicillin-Resistant Staphylococcus aureus (MRSA)
Título de la Revista: PROTEIN JOURNAL
Volumen: 38
Número: 5
Editorial: Springer
Fecha de publicación: 2019
Página de inicio: 506
Página final: 514
Idioma: English
DOI:

10.1007/s10930-019-09840-9

Notas: ISI, SCOPUS