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:	Paolo Grieco, Alfonso Carotenuto, Luigia Auriemma, Antonio Limatola, Salvatore Di Maro, Francesco Merlino, Maria Luisa Mangoni, Vincenzo Luca, Antonio Di Grazia, Stefano Gatti, Pietro Campiglia, Isabel Gomez-Monterrey, Ettore Novellino, Anna Catania
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c9559ba0ca774c489a775f9114627d36
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spelling	oai:doaj.org-article:c9559ba0ca774c489a775f9114627d362021-11-18T07:48:26ZNovel α-MSH peptide analogues with broad spectrum antimicrobial activity.1932-620310.1371/journal.pone.0061614https://doaj.org/article/c9559ba0ca774c489a775f9114627d362013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23626703/?tool=EBIhttps://doaj.org/toc/1932-6203Previous 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.Paolo GriecoAlfonso CarotenutoLuigia AuriemmaAntonio LimatolaSalvatore Di MaroFrancesco MerlinoMaria Luisa MangoniVincenzo LucaAntonio Di GraziaStefano GattiPietro CampigliaIsabel Gomez-MonterreyEttore NovellinoAnna CataniaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e61614 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Paolo Grieco Alfonso Carotenuto Luigia Auriemma Antonio Limatola Salvatore Di Maro Francesco Merlino Maria Luisa Mangoni Vincenzo Luca Antonio Di Grazia Stefano Gatti Pietro Campiglia Isabel Gomez-Monterrey Ettore Novellino Anna Catania Novel α-MSH peptide analogues with broad spectrum antimicrobial activity.
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.
format	article
author	Paolo Grieco Alfonso Carotenuto Luigia Auriemma Antonio Limatola Salvatore Di Maro Francesco Merlino Maria Luisa Mangoni Vincenzo Luca Antonio Di Grazia Stefano Gatti Pietro Campiglia Isabel Gomez-Monterrey Ettore Novellino Anna Catania
author_facet	Paolo Grieco Alfonso Carotenuto Luigia Auriemma Antonio Limatola Salvatore Di Maro Francesco Merlino Maria Luisa Mangoni Vincenzo Luca Antonio Di Grazia Stefano Gatti Pietro Campiglia Isabel Gomez-Monterrey Ettore Novellino Anna Catania
author_sort	Paolo Grieco
title	Novel α-MSH peptide analogues with broad spectrum antimicrobial activity.
title_short	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_sort	novel α-msh peptide analogues with broad spectrum antimicrobial activity.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/c9559ba0ca774c489a775f9114627d36
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Novel α-MSH peptide analogues with broad spectrum antimicrobial activity.

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