Structural and Functional Characterization of the Newly Designed Antimicrobial Peptide Crabrolin21
Francesca Cantini,
Paola Giannì,
Sara Bobone,
Cassandra Troiano,
Hugo van Ingen,
Renato Massoud,
Nicoletta Perini,
Luciana Migliore,
Philippe Savarin,
Charles Sanders,
Lorenzo Stella,
Marco Sette
Affiliations
Francesca Cantini
Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, 50019 Firenze, Italy
Paola Giannì
Department of Chemical Sciences and Technology, University of Rome Tor Vergata, 00133 Rome, Italy
Sara Bobone
Department of Chemical Sciences and Technology, University of Rome Tor Vergata, 00133 Rome, Italy
Cassandra Troiano
Department of Chemical Sciences and Technology, University of Rome Tor Vergata, 00133 Rome, Italy
Hugo van Ingen
NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands
Renato Massoud
Department of Experimental Medicine, University of Rome Tor Vergata, Viale della Ricerca Scientifica, 00133 Rome, Italy
Nicoletta Perini
Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy
Luciana Migliore
Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy
Philippe Savarin
Chemistry Structures Properties of Biomaterials and Therapeutic Agents Laboratory (CSPBAT), Nanomédecine Biomarqueurs Détection Team (NBD), Sorbonne Paris Nord University, The National Center for Scientific Research (CNRS), UMR 7244, 74 Rue Marcel Cachin, CEDEX, 93017 Bobigny, France
Charles Sanders
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA
Lorenzo Stella
Department of Chemical Sciences and Technology, University of Rome Tor Vergata, 00133 Rome, Italy
Marco Sette
Department of Chemical Sciences and Technology, University of Rome Tor Vergata, 00133 Rome, Italy
(1) Background: antimicrobial resistance is becoming a dramatic problem for public health, and the design of new antimicrobial agents is an active research area. (2) Methods: based on our previous work, we designed an improved version of the crabrolin peptide and characterized its functional and structural properties with a wide range of techniques. (3) Results: the newly designed peptide, crabrolin21, is much more active than the previous ones and shows specific selectivity towards bacterial cells. (4) Conclusions: crabrolin21 shows interesting properties and deserves further studies.