Peter Mergaert Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, France
1 protocol

Marco Scocchi Department of Life Sciences, University of Trieste, Italy
1 protocol

Mick Bourge Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, France
1 protocol

Olivier Pierre Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, France
1 protocol

Monica Benincasa
  • Department of Life Sciences, University of Trieste, Italy
Research focus
  • Microbiology
  • 1 Author merit


Ph.D in Biological Chemistry, Dept. of BBCM, University of Trieste, Italy, 2003

Current Position

Post-doctoral position in Biochemistry, Dept. of Life Sciences, University of Trieste, Italy

Publications (since 2010)

  1. Benincasa, M., Lagatolla, C., Dolzani, L., Milan, A., Pacor, S., Liut, G., Tossi, A., Cescutti, P. and Rizzo, R. (2016). Biofilms from Klebsiella pneumoniae: Matrix Polysaccharide Structure and Interactions with Antimicrobial Peptides. Microorganisms 4(3).
  2. Paulsen, V. S., Mardirossian, M., Blencke, H. M., Benincasa, M., Runti, G., Nepa, M., Haug, T., Stensvag, K. and Scocchi, M. (2016). Inner membrane proteins YgdD and SbmA are required for the complete susceptibility of E. coli to the proline-rich antimicrobial peptide arasin 1(1-25). Microbiology.
  3. Scocchi, M., Mardirossian, M., Runti, G. and Benincasa, M. (2016). Non-Membrane Permeabilizing Modes of Action of Antimicrobial Peptides on Bacteria. Curr Top Med Chem 16(1): 76-88.
  4. Xhindoli, D., Pacor, S., Benincasa, M., Scocchi, M., Gennaro, R. and Tossi, A. (2016). The human cathelicidin LL-37--A pore-forming antibacterial peptide and host-cell modulator. Biochim Biophys Acta 1858(3): 546-566.
  5. Benincasa, M., Francescon, M., Fregonese, M., Gennaro, R., Pengo, P., Rossi, P., Paolo Scrimin, P. and Tecilla, P. (2015). Helical peptide–polyamine and –polyether conjugates as synthetic ionophores. Bioorg Med Chem 23: 7386-7393.
  6. Gerdol, M., Puillandre, N., De Moro, G., Guarnaccia, C., Lucafo, M., Benincasa, M., Zlatev, V., Manfrin, C., Torboli, V., Giulianini, P. G., Sava, G., Venier, P. and Pallavicini, A. (2015). Identification and Characterization of a Novel Family of Cysteine-Rich Peptides (MgCRP-I) from Mytilus galloprovincialis. Genome Biol Evol 7(8): 2203-2219.
  7. Bociek, K., Ferluga, S., Mardirossian, M., Benincasa, M., Tossi, A., Gennaro, R. and Scocchi, M. (2015). Lipopolysaccharide Phosphorylation by the WaaY Kinase Affects the Susceptibility of Escherichia coli to the Human Antimicrobial Peptide LL-37. J Biol Chem 290(32): 19933-19941.
  8. Benincasa, M., Zahariev, S., Pelillo, C., Milan, A., Gennaro, R. and Scocchi, M. (2015). PEGylation of the peptide Bac7(1-35) reduces renal clearance while retaining antibacterial activity and bacterial cell penetration capacity. Eur J Med Chem 95: 210-219.
  9. Guida, F., Benincasa, M., Zahariev, S., Scocchi, M., Berti, F., Gennaro, R. and Tossi, A. (2015). Effect of size and N-terminal residue characteristics on bacterial cell penetration and antibacterial activity of the proline-rich peptide Bac7. J Med Chem 58(3): 1195-1204.
  10. Simunic, J., Petrov, D., Bouceba, T., Kamech, N., Benincasa, M. and Juretic, D. (2014). Trichoplaxin - a new membrane-active antimicrobial peptide from placozoan cDNA. Biochim Biophys Acta 1838(5): 1430-1438.
  11. Pelillo, C., Benincasa, M., Scocchi, M., Gennaro, R., Tossi, A. and Pacor, S. (2014). Cellular internalization and cytotoxicity of the antimicrobial proline-rich peptide Bac7(1-35) in monocytes/macrophages, and its activity against phagocytosed Salmonella typhimurium. Protein Pept Lett 21(4): 382-390.
  12. Runti, G., Lopez Ruiz Mdel, C., Stoilova, T., Hussain, R., Jennions, M., Choudhury, H. G., Benincasa, M., Gennaro, R., Beis, K. and Scocchi, M. (2013). Functional characterization of SbmA, a bacterial inner membrane transporter required for importing the antimicrobial peptide Bac7(1-35). J Bacteriol 195(23): 5343-5351.
  13. Paulsen, V. S., Blencke, H. M., Benincasa, M., Haug, T., Eksteen, J. J., Styrvold, O. B., Scocchi, M. and Stensvag, K. (2013). Structure-activity relationships of the antimicrobial peptide arasin 1 - and mode of action studies of the N-terminal, proline-rich region. PLoS One 8(1): e53326.
  14. Ilić, N., Novković, M., Guida, F., Xhindoli, D., Benincasa, M., Tossi, A. and Juretić, D. (2013). Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. BBA-Biomembranes 1828(3): 1004-1012.
  15. Donati, I., Benincasa, M., Foulc, M. P., Turco, G., Toppazzini, M., Solinas, D., Spilimbergo, S., Kikic, I. and Paoletti, S. (2012). Terminal sterilization of BisGMA-TEGDMA thermoset materials and their bioactive surfaces by supercritical CO2. Biomacromolecules 13(4): 1152-1160.
  16. Donati, M., Di Francesco, A., Di Paolo, M., Fiani, N., Benincasa, M., Gennaro, R., Nardini, P., Foschi, C. and Cevenini, R. (2011). Activity of Cathelicidin Peptides against Simkania negevensis. Int J Pept 2011: 708710.
  17. Benincasa, M., Pacor, S., Wu, W., Prato, M., Bianco, A. and Gennaro, R. (2011). Antifungal activity of amphotericin B conjugated to carbon nanotubes. ACS Nano 5(1): 199-208.
  18. Topazzini, M., Coslovi, A., Boschelle, M., Marsich, E., Benincasa, M., Gennaro, R. and Paoletti, S. (2011). Can the interaction between LL-37 and alginate be exploited for the formulation of new biomaterials with antimicrobial properties? Carbohydr Polym 83: 578-585.
  19. Travan, A., Marsich, E., Donati, I., Benincasa, M., Giazzon, M., Felisari, L. and Paoletti, S. (2011). Silver-polysaccharide nanocomposite antimicrobial coatings for methacrylic thermosets. Acta Biomater 7(1): 337-346.
  20. Marsich, E., Travan, A., Donati, I., Di Luca, A., Benincasa, M., Crosera, M. and Paoletti, S. (2011). Biological response of hydrogels embedding gold nanoparticles. Colloids Surf B Biointerfaces 83(2): 331-339.
  21. Benincasa, M., Pelillo, C., Zorzet, S., Garrovo, C., Biffi, S., Gennaro, R. and Scocchi, M. (2010). The proline-rich peptide Bac7(1-35) reduces mortality from Salmonella typhimurium in a mouse model of infection. BMC Microbiol 10: 178.
  22. Donati, M., Di Francesco, A., Gennaro, R., Benincasa, M., Di Paolo, M., Shurdhi, A., Ostanello, F., Baldelli, R. and Cevenini, R. (2010). Increasing effect of a high dose of PG-1 peptide on the infectivity of Chlamydophila abortus. FEMS Immunol Med Microbiol 59(2): 221-222.
  23. Wehmeier, S., Arnold, M. F., Marlow, V. L., Aouida, M., Myka, K., Fletcher, V., Benincasa, M., Scocchi, M., Ramatar, D. and Ferguson, G. (2010). Internalisation of a thiazole-modified peptide in Sinorhizobium meliloti occurs by BacA-dependent and -independent mechanisms. Microbiology 156: 2702-2713.
  24. Tomasinsig, L., Benincasa, M., Scocchi, M., Skerlavaj, B., Tossi, A., Zanetti, M. and Gennaro, R. (2010). Role of Cathelicidin Peptides in Bovine Host Defense and Healing. Probiotics Antimicrob Proteins 2(1): 12-20.
  25. Comegna, D., Benincasa, M., Gennaro, R., Izzo, I. and De Riccardis, F. (2010). Design, synthesis and antimicrobial properties of non-hemolytic cationic alpha-cyclopeptoids. Bioorg Med Chem 18(5): 2010-2018.
1 Protocol published
Antimicrobial peptides (AMPs) can target the bacterial envelope or alternatively have intracellular targets. The latter requires uptake of the peptide by the bacterial cells. The bacterial internalization of an AMP can be evaluated by a ...
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