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Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity

Previous investigations indicate that α-melanocyte-stimulating hormone (α-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...

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Autores principales: Grieco, Paolo, Carotenuto, Alfonso, Auriemma, Luigia, Limatola, Antonio, Di Maro, Salvatore, Merlino, Francesco, Mangoni, Maria Luisa, Luca, Vincenzo, Di Grazia, Antonio, Gatti, Stefano, Campiglia, Pietro, Gomez-Monterrey, Isabel, Novellino, Ettore, Catania, Anna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634028/
https://www.ncbi.nlm.nih.gov/pubmed/23626703
http://dx.doi.org/10.1371/journal.pone.0061614
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author Grieco, Paolo
Carotenuto, Alfonso
Auriemma, Luigia
Limatola, Antonio
Di Maro, Salvatore
Merlino, Francesco
Mangoni, Maria Luisa
Luca, Vincenzo
Di Grazia, Antonio
Gatti, Stefano
Campiglia, Pietro
Gomez-Monterrey, Isabel
Novellino, Ettore
Catania, Anna
author_facet Grieco, Paolo
Carotenuto, Alfonso
Auriemma, Luigia
Limatola, Antonio
Di Maro, Salvatore
Merlino, Francesco
Mangoni, Maria Luisa
Luca, Vincenzo
Di Grazia, Antonio
Gatti, Stefano
Campiglia, Pietro
Gomez-Monterrey, Isabel
Novellino, Ettore
Catania, Anna
author_sort Grieco, Paolo
collection PubMed
description Previous investigations indicate that α-melanocyte-stimulating hormone (α-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 α-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.
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spelling pubmed-36340282013-04-26 Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity Grieco, Paolo Carotenuto, Alfonso Auriemma, Luigia Limatola, Antonio Di Maro, Salvatore Merlino, Francesco Mangoni, Maria Luisa Luca, Vincenzo Di Grazia, Antonio Gatti, Stefano Campiglia, Pietro Gomez-Monterrey, Isabel Novellino, Ettore Catania, Anna PLoS One Research Article Previous investigations indicate that α-melanocyte-stimulating hormone (α-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 α-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. Public Library of Science 2013-04-23 /pmc/articles/PMC3634028/ /pubmed/23626703 http://dx.doi.org/10.1371/journal.pone.0061614 Text en © 2013 Grieco et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Grieco, Paolo
Carotenuto, Alfonso
Auriemma, Luigia
Limatola, Antonio
Di Maro, Salvatore
Merlino, Francesco
Mangoni, Maria Luisa
Luca, Vincenzo
Di Grazia, Antonio
Gatti, Stefano
Campiglia, Pietro
Gomez-Monterrey, Isabel
Novellino, Ettore
Catania, Anna
Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
title Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
title_full Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
title_fullStr Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
title_full_unstemmed Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
title_short Novel α-MSH Peptide Analogues with Broad Spectrum Antimicrobial Activity
title_sort novel α-msh peptide analogues with broad spectrum antimicrobial activity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634028/
https://www.ncbi.nlm.nih.gov/pubmed/23626703
http://dx.doi.org/10.1371/journal.pone.0061614
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