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Novel formulation of antimicrobial peptides enhances antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA).
Faya, Mbuso; Hazzah, Heba A; Omolo, Calvin A; Agrawal, Nikhi; Maji, Ruma; Walvekar, Pavan; Mocktar, Chunderika; Nkambule, Bongani; Rambharose, Sanjeev; Albericio, Fernando; de la Torre, Beatriz G; Govender, Thirumala.
Afiliación
  • Faya M; Discipline of Pharmaceutical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • Hazzah HA; Peptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, Durban, 4001, South Africa.
  • Omolo CA; KwaZulu-Natal Research Innovation and Sequencing Platform (KRISP), School of Laboratory Medicine and Medical Sciences, College of Health Sciences, University of KwaZulu-Natal Durban, Durban, 4041, South Africa.
  • Agrawal N; Discipline of Pharmaceutical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • Maji R; Department of Pharmaceutics, School of Pharmacy and Health Sciences, United States International University-Africa, P. O. Box 14634-00800, Nairobi, Kenya.
  • Walvekar P; Discipline of Pharmaceutical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • Mocktar C; Discipline of Pharmaceutical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • Nkambule B; Discipline of Pharmaceutical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • Rambharose S; Discipline of Pharmaceutical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • Albericio F; School of Laboratory Medicine and Medical Sciences, College of Health Sciences, University of KwaZulu-Natal, Private Bag, Durban, X54001, South Africa.
  • de la Torre BG; Department of Surgery, Division of Emergency Medicine, University of Cape Town, Cape Town, South Africa.
  • Govender T; Peptide Science Laboratory, School of Chemistry and Physics, University of KwaZulu-Natal, Durban, 4001, South Africa.
Amino Acids ; 52(10): 1439-1457, 2020 Oct.
Article en En | MEDLINE | ID: mdl-33074344
Antimicrobial peptides (AMPs) have the ability to penetrate as well as transport cargo across bacterial cell membranes, and they have been labeled as exceptional candidates to function in drug delivery. The aim of this study was to investigate the effectiveness of novel formulation of AMPs for enhanced MRSA activity. The strategy was carried out through the formulation of liposomes by thin-layer film hydration methodology, containing phosphatidylcholine, cholesterol, oleic acid, the novel AMP, as well as vancomycin (VCM). Characterization of the AMPs and liposomes included HPLC and LCMS for peptide purity and mass determination; DLS (size, polydispersity, zeta potential), TEM (surface morphology), dialysis (drug release), broth dilution, and flow cytometry (antibacterial activity); MTT assay, haemolysis and intracellular antibacterial studies. The size, PDI, and zeta potential of the drug-loaded AMP2-Lipo-1 were 102.6 ± 1.81 nm, 0.157 ± 0.01, and - 9.81 ± 1.69 mV, respectively, while for AMP3-Lipo-2 drug-loaded formulation, it was 146.4 ± 1.90 nm, 0.412 ± 0.05, and - 4.27 ± 1.25 mV respectively at pH 7.4. However, in acidic pH for both formulations, we observed an increase in size, PDI, and a switch to positive zeta potential, which indicated the pH responsiveness of our liposomal systems. The in vitro drug release studies demonstrated that liposomal formulations released VCM-HCl at a faster rate at pH 6.0 compared to pH 7.4. In vitro antibacterial activity against S. aureus and MRSA revealed that liposomes had enhanced activity at pH 6 compared to pH 7.4. The study revealed that the formulation can potentially be used to enhance activity and penetration of AMPs, thereby improving the treatment of bacterial infections.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Citotóxicas Formadoras de Poros / Staphylococcus aureus Resistente a Meticilina / Antibacterianos Límite: Humans Idioma: En Revista: Amino Acids Asunto de la revista: BIOQUIMICA Año: 2020 Tipo del documento: Article País de afiliación: Sudáfrica Pais de publicación: Austria
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Citotóxicas Formadoras de Poros / Staphylococcus aureus Resistente a Meticilina / Antibacterianos Límite: Humans Idioma: En Revista: Amino Acids Asunto de la revista: BIOQUIMICA Año: 2020 Tipo del documento: Article País de afiliación: Sudáfrica Pais de publicación: Austria