Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.

The branched M33 antimicrobial peptide was previously shown to be very active against Gram-negative bacterial pathogens, including multidrug-resistant strains. In an attempt to produce back-up molecules, we synthesized an M33 peptide isomer consisting of D-aminoacids (M33-D). This isomeric version s...

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Autores principales:	Chiara Falciani, Luisa Lozzi, Simona Pollini, Vincenzo Luca, Veronica Carnicelli, Jlenia Brunetti, Barbara Lelli, Stefano Bindi, Silvia Scali, Antonio Di Giulio, Gian Maria Rossolini, Maria Luisa Mangoni, Luisa Bracci, Alessandro Pini
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6fa108c5020d4f499fc5bcf653798a8e
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spelling	oai:doaj.org-article:6fa108c5020d4f499fc5bcf653798a8e2021-11-18T08:13:29ZIsomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.1932-620310.1371/journal.pone.0046259https://doaj.org/article/6fa108c5020d4f499fc5bcf653798a8e2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23056272/?tool=EBIhttps://doaj.org/toc/1932-6203The branched M33 antimicrobial peptide was previously shown to be very active against Gram-negative bacterial pathogens, including multidrug-resistant strains. In an attempt to produce back-up molecules, we synthesized an M33 peptide isomer consisting of D-aminoacids (M33-D). This isomeric version showed 4 to 16-fold higher activity against Gram-positive pathogens, including Staphylococcus aureus and Staphylococcus epidermidis, than the original peptide, while retaining strong activity against Gram-negative bacteria. The antimicrobial activity of both peptides was influenced by their differential sensitivity to bacterial proteases. The better activity shown by M33-D against S. aureus compared to M33-L was confirmed in biofilm eradication experiments where M33-L showed 12% activity with respect to M33-D, and in vivo models where Balb-c mice infected with S. aureus showed 100% and 0% survival when treated with M33-D and M33-L, respectively. M33-D appears to be an interesting candidate for the development of novel broad-spectrum antimicrobials active against bacterial pathogens of clinical importance.Chiara FalcianiLuisa LozziSimona PolliniVincenzo LucaVeronica CarnicelliJlenia BrunettiBarbara LelliStefano BindiSilvia ScaliAntonio Di GiulioGian Maria RossoliniMaria Luisa MangoniLuisa BracciAlessandro PiniPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e46259 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chiara Falciani Luisa Lozzi Simona Pollini Vincenzo Luca Veronica Carnicelli Jlenia Brunetti Barbara Lelli Stefano Bindi Silvia Scali Antonio Di Giulio Gian Maria Rossolini Maria Luisa Mangoni Luisa Bracci Alessandro Pini Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
description	The branched M33 antimicrobial peptide was previously shown to be very active against Gram-negative bacterial pathogens, including multidrug-resistant strains. In an attempt to produce back-up molecules, we synthesized an M33 peptide isomer consisting of D-aminoacids (M33-D). This isomeric version showed 4 to 16-fold higher activity against Gram-positive pathogens, including Staphylococcus aureus and Staphylococcus epidermidis, than the original peptide, while retaining strong activity against Gram-negative bacteria. The antimicrobial activity of both peptides was influenced by their differential sensitivity to bacterial proteases. The better activity shown by M33-D against S. aureus compared to M33-L was confirmed in biofilm eradication experiments where M33-L showed 12% activity with respect to M33-D, and in vivo models where Balb-c mice infected with S. aureus showed 100% and 0% survival when treated with M33-D and M33-L, respectively. M33-D appears to be an interesting candidate for the development of novel broad-spectrum antimicrobials active against bacterial pathogens of clinical importance.
format	article
author	Chiara Falciani Luisa Lozzi Simona Pollini Vincenzo Luca Veronica Carnicelli Jlenia Brunetti Barbara Lelli Stefano Bindi Silvia Scali Antonio Di Giulio Gian Maria Rossolini Maria Luisa Mangoni Luisa Bracci Alessandro Pini
author_facet	Chiara Falciani Luisa Lozzi Simona Pollini Vincenzo Luca Veronica Carnicelli Jlenia Brunetti Barbara Lelli Stefano Bindi Silvia Scali Antonio Di Giulio Gian Maria Rossolini Maria Luisa Mangoni Luisa Bracci Alessandro Pini
author_sort	Chiara Falciani
title	Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
title_short	Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
title_full	Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
title_fullStr	Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
title_full_unstemmed	Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
title_sort	isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/6fa108c5020d4f499fc5bcf653798a8e
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Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.

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