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Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin

BACKGROUND: hGlyrichin is a novel human antimicrobial peptide rich in glycine. The previous study of known human antimicrobial peptides indicated that in an eligible range, the greater corresponding antibacterial activity was consisted with the shorter peptide sequence. FINDINGS: Two peptides named...

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Detalles Bibliográficos
Autores principales: Sha, Jibin, Zhang, Chenggang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4993737/
https://www.ncbi.nlm.nih.gov/pubmed/27610301
http://dx.doi.org/10.1186/s40064-016-3025-4
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author Sha, Jibin
Zhang, Chenggang
author_facet Sha, Jibin
Zhang, Chenggang
author_sort Sha, Jibin
collection PubMed
description BACKGROUND: hGlyrichin is a novel human antimicrobial peptide rich in glycine. The previous study of known human antimicrobial peptides indicated that in an eligible range, the greater corresponding antibacterial activity was consisted with the shorter peptide sequence. FINDINGS: Two peptides named pCM19 and pCM12 were synthesized and the antibacterial activity assay results showed that these peptides exhibited strong antibacterial activity that was inversely proportional to the length of the peptide. Despite the effective inhibition of bacterial growth, the synthetic peptides showed no hemolytic effect on human red blood cells. CONCLUSIONS: Taken together, these two peptides derived from hGlyrichin both have strong antibacterial activity and are not toxic to human somatic cells.
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spelling pubmed-49937372016-09-08 Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin Sha, Jibin Zhang, Chenggang Springerplus Short Report BACKGROUND: hGlyrichin is a novel human antimicrobial peptide rich in glycine. The previous study of known human antimicrobial peptides indicated that in an eligible range, the greater corresponding antibacterial activity was consisted with the shorter peptide sequence. FINDINGS: Two peptides named pCM19 and pCM12 were synthesized and the antibacterial activity assay results showed that these peptides exhibited strong antibacterial activity that was inversely proportional to the length of the peptide. Despite the effective inhibition of bacterial growth, the synthetic peptides showed no hemolytic effect on human red blood cells. CONCLUSIONS: Taken together, these two peptides derived from hGlyrichin both have strong antibacterial activity and are not toxic to human somatic cells. Springer International Publishing 2016-08-22 /pmc/articles/PMC4993737/ /pubmed/27610301 http://dx.doi.org/10.1186/s40064-016-3025-4 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Short Report
Sha, Jibin
Zhang, Chenggang
Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin
title Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin
title_full Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin
title_fullStr Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin
title_full_unstemmed Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin
title_short Antibacterial activity identification of pCM19 and pCM12 derived from hGlyrichin
title_sort antibacterial activity identification of pcm19 and pcm12 derived from hglyrichin
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4993737/
https://www.ncbi.nlm.nih.gov/pubmed/27610301
http://dx.doi.org/10.1186/s40064-016-3025-4
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