http://www.cnr.it/ontology/cnr/individuo/prodotto/ID15927

Substitution of the Arginine/Leucine Residues in Apidaecin Ib with Peptoid Residues: Effect on Antimicrobial Activity, Cellular Uptake, and Proteolytic Degradation (Articolo in rivista)

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Substitution of the Arginine/Leucine Residues in Apidaecin Ib with Peptoid Residues: Effect on Antimicrobial Activity, Cellular Uptake, and Proteolytic Degradation (Articolo in rivista) (literal)

Anno

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Alternative label

Marina Gobbo; Monica Benincasa; Giulio Bertoloni; Barbara Biondi; Ryan Dosselli; Emanuele Papini; Elena Reddi; Raniero Rocchi; Regina Tavano; Renato Gennaro (2009)
Substitution of the Arginine/Leucine Residues in Apidaecin Ib with Peptoid Residues: Effect on Antimicrobial Activity, Cellular Uptake, and Proteolytic Degradation
in Journal of medicinal chemistry
(literal)

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Marina Gobbo; Monica Benincasa; Giulio Bertoloni; Barbara Biondi; Ryan Dosselli; Emanuele Papini; Elena Reddi; Raniero Rocchi; Regina Tavano; Renato Gennaro (literal)

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Department of Chemical Sciences, University of Padova, Via Marzolo, 1, 35131 Padova, Italy; Department of Life Sciences, University of Trieste, Via Giorgeri 1, 34127 Trieste, Italy; Department of Histology, Microbiology, and Medical Biotechnology, University of Padova, Via Gabelli 63, 35131 Padova, Italy; Institute of Biomolecular Chemistry of C.N.R., Via Marzolo, 1, 35131 Padova, Italy; Department of Biology, University of Padova, Via Bassi 1/B, 35121 Padova, Italy; C.R.I.B.I. and Department of Biomedical Sciences, University of Padova, Via Bassi 1/B, 35121 Padova, Italy (literal)

Titolo

Substitution of the Arginine/Leucine Residues in Apidaecin Ib with Peptoid Residues: Effect on Antimicrobial Activity, Cellular Uptake, and Proteolytic Degradation (literal)

Abstract

Several aspects of the mechanism of action of Pro-rich antimicrobial peptides, together with their low toxicity ill mammalian cells, make them good candidates for the development of new antibiotic agents. We investigated the effect induced in the insect antimicrobial peptide apidaecin Ib by the replacement of a single arginine/leucine residue witha N-substituted glycine. The resulting peptoid-peptide hybrids are more resistant to proteolysis and devoid of any significant cytotoxic activity, but moving the [NArg]residue from the N- to the C-terminal end of the molecule progressively reduces the antibacterial activity. Cell uptake experiments in E. coli cells suggest that the loss of antibacterial activity of [NArg(17)]apidaecin is a consequence of its inability to translocate into bacterial cells. Conversely, apidaecin and its peptoid-peptide hybrids are able to cross the plasma membrane ill eukaryotic cells and to diffuse in the cytosol, although their translocating ability is far less effective than that of other known cell permeant peptides. (literal)

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