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Enhanced antimicrobial activity of a peptide derived from human lysozyme by arylation of its tryptophan residues.
González, Rodrigo; Mendive-Tapia, Lorena; Pastrian, María B; Albericio, Fernando; Lavilla, Rodolfo; Cascone, Osvaldo; Iannucci, Nancy B.
Afiliação
  • González R; Cathedra of Biotechnology, School of Pharmacy and Biochemistry, UBA, and NANOBIOTEC, UBA-CONICET, Junín 956, (1113), Buenos Aires, Argentina.
  • Mendive-Tapia L; Department of Organic Chemistry, School of Chemistry, University of Barcelona, Martí i Franquès 1-11, 08028, Barcelona, Spain.
  • Pastrian MB; Institute for Research in Biomedicine, Barcelona Science Park, Baldiri Reixac 10, 08028, Barcelona, Spain.
  • Albericio F; CIBER-BBN, Networking Centre on Bioengineering, Biomaterials and Nanomedicine, Barcelona Science Park, Baldiri Reixac 10, 08028, Barcelona, Spain.
  • Lavilla R; Cathedra of Biotechnology, School of Pharmacy and Biochemistry, UBA, and NANOBIOTEC, UBA-CONICET, Junín 956, (1113), Buenos Aires, Argentina.
  • Cascone O; Department of Organic Chemistry, School of Chemistry, University of Barcelona, Martí i Franquès 1-11, 08028, Barcelona, Spain.
  • Iannucci NB; Institute for Research in Biomedicine, Barcelona Science Park, Baldiri Reixac 10, 08028, Barcelona, Spain.
J Pept Sci ; 22(2): 123-8, 2016 Feb.
Article em En | MEDLINE | ID: mdl-26785822
Antimicrobial peptides are valuable agents to fight antibiotic resistance. These amphipatic species display positively charged and hydrophobic amino acids. Here, we enhance the local hydrophobicity of a model peptide derived from human lysozyme (107RKWVWWRNR115) by arylation of its tryptophan (Trp) residues, which renders a positive effect on Staphylococcus aureus and Staphylococcus epidermidis growth inhibition. This site-selective modification was accessed by solid-phase peptide synthesis using the non-proteinogenic amino acid 2-aryltryptophan, generated by direct C-H activation from protected Trp. The modification brought about a relevant increase in growth inhibition: S. aureus was fully inhibited by arylation of Trp 112 and by only 10% by arylation of Trp 109 or 111, respect to the non-arylated peptide. On the other hand, S. epidermidis was fully inhibited by the three arylated peptides and the parent peptide. The minimum inhibitory concentration was significantly reduced for S. aureus depending on the arylation site.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Triptofano / Muramidase / Antibacterianos Limite: Humans Idioma: En Revista: J Pept Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Triptofano / Muramidase / Antibacterianos Limite: Humans Idioma: En Revista: J Pept Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Argentina País de publicação: Reino Unido