Marco Scocchi

Summary

Affiliation: University of Trieste
Country: Italy

Publications

  1. doi request reprint The salmonid cathelicidins: a gene family with highly varied C-terminal antimicrobial domains
    Marco Scocchi
    Department of Life Sciences, University of Trieste, Italy
    Comp Biochem Physiol B Biochem Mol Biol 152:376-81. 2009
  2. doi request reprint Investigating the mode of action of proline-rich antimicrobial peptides using a genetic approach: a tool to identify new bacterial targets amenable to the design of novel antibiotics
    Marco Scocchi
    Department of Life Sciences, University of Trieste, Trieste, Italy
    Methods Mol Biol 494:161-76. 2008
  3. pmc Functional characterization of SbmA, a bacterial inner membrane transporter required for importing the antimicrobial peptide Bac7(1-35)
    Giulia Runti
    Department of Life Sciences, University of Trieste, Trieste, Italy
    J Bacteriol 195:5343-51. 2013
  4. ncbi request reprint Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides
    Maura Mattiuzzo
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    Mol Microbiol 66:151-63. 2007
  5. ncbi request reprint Fungicidal activity of five cathelicidin peptides against clinically isolated yeasts
    Monica Benincasa
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, 34127 Trieste, Italy
    J Antimicrob Chemother 58:950-9. 2006
  6. pmc Rapid and reliable detection of antimicrobial peptide penetration into gram-negative bacteria based on fluorescence quenching
    Monica Benincasa
    Department of Life Sciences, University of Trieste, 34127 Trieste, Italy
    Antimicrob Agents Chemother 53:3501-4. 2009
  7. pmc Lipopolysaccharide Phosphorylation by the WaaY Kinase Affects the Susceptibility of Escherichia coli to the Human Antimicrobial Peptide LL-37
    Karol Bociek
    From the Department of Life Sciences, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    J Biol Chem 290:19933-41. 2015
  8. ncbi request reprint Dual mode of action of Bac7, a proline-rich antibacterial peptide
    Elena Podda
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    Biochim Biophys Acta 1760:1732-40. 2006
  9. doi request reprint PEGylation of the peptide Bac7(1-35) reduces renal clearance while retaining antibacterial activity and bacterial cell penetration capacity
    Monica Benincasa
    Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127 Trieste, Italy
    Eur J Med Chem 95:210-9. 2015
  10. doi request reprint Effect of size and N-terminal residue characteristics on bacterial cell penetration and antibacterial activity of the proline-rich peptide Bac7
    Filomena Guida
    Department of Life Sciences and Department of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste I 34127, Italy
    J Med Chem 58:1195-204. 2015

Collaborators

Detail Information

Publications17

  1. doi request reprint The salmonid cathelicidins: a gene family with highly varied C-terminal antimicrobial domains
    Marco Scocchi
    Department of Life Sciences, University of Trieste, Italy
    Comp Biochem Physiol B Biochem Mol Biol 152:376-81. 2009
    ..The high variation in length and sequence of this region suggests the existence of a genetically unstable region similar to that found in some mammalian cathelicidins...
  2. doi request reprint Investigating the mode of action of proline-rich antimicrobial peptides using a genetic approach: a tool to identify new bacterial targets amenable to the design of novel antibiotics
    Marco Scocchi
    Department of Life Sciences, University of Trieste, Trieste, Italy
    Methods Mol Biol 494:161-76. 2008
    ....
  3. pmc Functional characterization of SbmA, a bacterial inner membrane transporter required for importing the antimicrobial peptide Bac7(1-35)
    Giulia Runti
    Department of Life Sciences, University of Trieste, Trieste, Italy
    J Bacteriol 195:5343-51. 2013
    ..Overall, these results shed light on the SbmA-mediated internalization of peptide substrates and suggest that the transport of an unknown substrate(s) represents the function of this protein. ..
  4. ncbi request reprint Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides
    Maura Mattiuzzo
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    Mol Microbiol 66:151-63. 2007
    ....
  5. ncbi request reprint Fungicidal activity of five cathelicidin peptides against clinically isolated yeasts
    Monica Benincasa
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, 34127 Trieste, Italy
    J Antimicrob Chemother 58:950-9. 2006
    ..To investigate the in vitro antifungal activity of the structurally different cathelicidin peptides SMAP-29, BMAP-27, BMAP-28, protegrin-1 (PG-1) and indolicidin...
  6. pmc Rapid and reliable detection of antimicrobial peptide penetration into gram-negative bacteria based on fluorescence quenching
    Monica Benincasa
    Department of Life Sciences, University of Trieste, 34127 Trieste, Italy
    Antimicrob Agents Chemother 53:3501-4. 2009
    ..Identification of peptides with the former mechanism is of considerable interest for the intracellular delivery of membrane-impermeant drugs...
  7. pmc Lipopolysaccharide Phosphorylation by the WaaY Kinase Affects the Susceptibility of Escherichia coli to the Human Antimicrobial Peptide LL-37
    Karol Bociek
    From the Department of Life Sciences, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    J Biol Chem 290:19933-41. 2015
    ....
  8. ncbi request reprint Dual mode of action of Bac7, a proline-rich antibacterial peptide
    Elena Podda
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    Biochim Biophys Acta 1760:1732-40. 2006
    ....
  9. doi request reprint PEGylation of the peptide Bac7(1-35) reduces renal clearance while retaining antibacterial activity and bacterial cell penetration capacity
    Monica Benincasa
    Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127 Trieste, Italy
    Eur J Med Chem 95:210-9. 2015
    ..This can be an equally important issue to reducing cytotoxicity for therapeutic use of these antibacterials. ..
  10. doi request reprint Effect of size and N-terminal residue characteristics on bacterial cell penetration and antibacterial activity of the proline-rich peptide Bac7
    Filomena Guida
    Department of Life Sciences and Department of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste I 34127, Italy
    J Med Chem 58:1195-204. 2015
    ..Our studies allowed building a more detailed model for the mode-of-action of Bac7, and confirming its potential as an anti-infective agent, also suggesting it may be a vehicle for internalization of other antibiotic cargo. ..
  11. ncbi request reprint Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides
    Maura Mattiuzzo
    Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127 Trieste, Italy
    J Microbiol Biotechnol 24:160-7. 2014
    ..coli OpdB...
  12. pmc The proline-rich peptide Bac7(1-35) reduces mortality from Salmonella typhimurium in a mouse model of infection
    Monica Benincasa
    Department of Life Sciences, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy
    BMC Microbiol 10:178. 2010
    ..Bac7 is a proline-rich peptide with a potent in vitro antimicrobial activity against Gram-negative bacteria. Here we investigated its activity in biological fluids and in vivo using a mouse model of S. typhimurium infection...
  13. ncbi request reprint Structural aspects of plant antimicrobial peptides
    Lara Padovan
    Genetic Service, IRCCS Burlo Garofolo and Department of Developmental and Reproductive Sciences, University of Trieste, 34137 Trieste, Italy
    Curr Protein Pept Sci 11:210-9. 2010
    ..This extends their interest from defense of important food crops also to the design of novel anti-infective compounds for both pharmaceutical and agricultural applications...
  14. ncbi request reprint Antimicrobial activity of Bac7 fragments against drug-resistant clinical isolates
    Monica Benincasa
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri, 1, I 34127 Trieste, Italy
    Peptides 25:2055-61. 2004
    ..In addition, when tested against fungi, the longer fragment was also active against collection strains and clinical isolates of Cryptococcus neoformans, but not towards clinical isolates of Candida albicans...
  15. doi request reprint The host antimicrobial peptide Bac71-35 binds to bacterial ribosomal proteins and inhibits protein synthesis
    Mario Mardirossian
    Department of Life Sciences, University of Trieste, Via Giorgieri 5, Trieste 34127, Italy
    Chem Biol 21:1639-47. 2014
    ..Overall, these results indicate that the killing mechanism of Bac71-35 is based on a specific block of protein synthesis. ..
  16. doi request reprint Use of unnatural amino acids to probe structure-activity relationships and mode-of-action of antimicrobial peptides
    Alessandro Tossi
    Department of Life Sciences, University of Trieste, Trieste, Italy
    Methods Mol Biol 794:169-83. 2012
    ..Here, we describe how such residues can be used to modulate such key parameters as cationicity, hydrophobicity, steric factors conformational stability, and H-bonding...
  17. ncbi request reprint Structural aspects and biological properties of the cathelicidin PMAP-36
    Marco Scocchi
    Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Italy
    FEBS J 272:4398-406. 2005
    ..It allows the molecule to achieve an impressive charge density (+28 in 70 residues), although the significance of this feature with respect to biological activity has yet to be determined...