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3 results on '"Di Maro, Salvatore"'

1. Properly Substituted Analogues of BIX-01294 Lose Inhibition of G9a Histone Methyltransferase and Gain Selective Anti-DNA Methyltransferase 3A Activity

Author

Rotili, Dante, primary, Tarantino, Domenico, additional, Marrocco, Biagina, additional, Gros, Christina, additional, Masson, Véronique, additional, Poughon, Valérie, additional, Ausseil, Fréderic, additional, Chang, Yanqi, additional, Labella, Donatella, additional, Cosconati, Sandro, additional, Di Maro, Salvatore, additional, Novellino, Ettore, additional, Schnekenburger, Michael, additional, Grandjenette, Cindy, additional, Bouvy, Celine, additional, Diederich, Marc, additional, Cheng, Xiaodong, additional, Arimondo, Paola B., additional, and Mai, Antonello, additional

Published
2014
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2. Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity

Author

Grieco, Paolo, primary, Carotenuto, Alfonso, additional, Auriemma, Luigia, additional, Limatola, Antonio, additional, Di Maro, Salvatore, additional, Merlino, Francesco, additional, Mangoni, Maria Luisa, additional, Luca, Vincenzo, additional, Di Grazia, Antonio, additional, Gatti, Stefano, additional, Campiglia, Pietro, additional, Gomez-Monterrey, Isabel, additional, Novellino, Ettore, additional, and Catania, Anna, additional

Published
2013
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3. Novel α-MSH peptide analogues with broad spectrum antimicrobial activity

Author

Luigia Auriemma, Stefano Gatti, Ettore Novellino, Anna Catania, Vincenzo Luca, Antonio Limatola, Pietro Campiglia, Isabel Gomez-Monterrey, Paolo Grieco, Francesco Merlino, Salvatore Di Maro, Maria Luisa Mangoni, Antonio Di Grazia, Alfonso Carotenuto, Grieco, Paolo, Carotenuto, Alfonso, L., Auriemma, Limatola, Antonio, DI MARO, Salvatore, Merlino, Francesco, M. L., Mangoni, V., Luca, A., Di Grazia, S., Gatti, P., Campiglia, GOMEZ MONTERREY, ISABEL MARIA, Novellino, Ettore, A., Catania, Grieco, P., Carotenuto, A., Auriemma, L., Limatola, A., Di Maro, S., Merlino, F., Mangoni, M. L., Luca, V., Di Grazia, A., Gatti, S., Campiglia, P., Gomez-Monterrey, I., Novellino, E., and Catania, A.

Subjects
Anti-Infective Agent, Candida albican, Keratinocytes, Models, Molecular, Proteomics, Erythrocytes, Solid-Phase Synthesis Technique, Peptide, Candida glabrata, chemistry.chemical_compound, Anti-Infective Agents, Candida albicans, Drug Discovery, Peptide synthesis, Macromolecular Structure Analysis, Candida, chemistry.chemical_classification, Multidisciplinary, biology, Microbial Sensitivity Test, Biological activity, Antimicrobial, temporin L, Erythrocyte, Chemistry, Biochemistry, Oligopeptide, Medicine, Oligopeptides, amino acid, Keratinocyte, Human, Research Article, Biotechnology, spectroscopy, Hemolysi, Drugs and Devices, Gram-negative bacteria, Drug Research and Development, Cell Survival, Science, Microbial Sensitivity Tests, Mycology, Gram-Positive Bacteria, Hemolysis, Microbiology, Cell Line, side chains, Structure-Activity Relationship, anticandida, Gram-Negative Bacteria, Structure–activity relationship, Humans, Synthetic Peptide, selectivity, candidacidal activity, melanocyte-stimulating hormone, Biology, Solid-Phase Synthesis Techniques, Molecular Mimicry, Computational Biology, Bacteriology, NMR conformational analysi, biology.organism_classification, Yeast, chemistry, Pharmacodynamics, alpha-MSH, antimicrobial, Medicinal Chemistry
Abstract

Previous investigations indicate that alpha-melanocyte-stimulating hormone (alpha-MSH) and certain synthetic analogues of it exert antimicrobial effects against bacteria and yeasts. However, these molecules have weak activity in standard microbiology conditions and this hampers a realistic clinical use. The aim in the present study was to identify novel peptides with broad-spectrum antimicrobial activity in growth medium. To this purpose, the Gly10 residue in the [DNal(2')-7,Phe-12]-MSH(6-13) sequence was replaced with conventional and unconventional amino acids with different degrees of conformational rigidity. Two derivatives in which Gly10 was replaced by the residues Aic and Cha, respectively, had substantial activity against Candida strains, including C. albicans, C. glabrata, and C. krusei and against gram-positive and gram-negative bacteria. Conformational analysis indicated that the helical structure along residues 8-13 is a key factor in antimicrobial activity. Synthetic analogues of alpha-MSH can be valuable agents to treat infections in humans. The structural preferences associated with antimicrobial activity identified in this research can help further development of synthetic melanocortins with enhanced biological activity.

Published
2013

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