Peptide oligomers from ultra-short peptides using sortase

Sortase A catalyzed ligation of ultra-short peptides leads to inter/intra-molecular transpeptidation to form either linear or cyclic oligomers dependent upon the peptide length. Cyclic peptides were the main products for peptides with more than 15aa. However, for ultra-short (<15aa) peptides, cyc...

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Detalles Bibliográficos
Autores principales: Voloshchuk, Natalya, Chen, Long, Li, Qiang, Liang, Jun F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5614665/
https://www.ncbi.nlm.nih.gov/pubmed/28955731
http://dx.doi.org/10.1016/j.bbrep.2017.02.005
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author Voloshchuk, Natalya
Chen, Long
Li, Qiang
Liang, Jun F.
author_facet Voloshchuk, Natalya
Chen, Long
Li, Qiang
Liang, Jun F.
author_sort Voloshchuk, Natalya
collection PubMed
description Sortase A catalyzed ligation of ultra-short peptides leads to inter/intra-molecular transpeptidation to form either linear or cyclic oligomers dependent upon the peptide length. Cyclic peptides were the main products for peptides with more than 15aa. However, for ultra-short (<15aa) peptides, cyclic oligomers became predominant in prolonged reactions. Peptides with 1–3 aminoglycines were equally active but peptide oligomers from peptide containing more than one aminoglycine were prone to hydrolysis.
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spelling pubmed-56146652017-09-27 Peptide oligomers from ultra-short peptides using sortase Voloshchuk, Natalya Chen, Long Li, Qiang Liang, Jun F. Biochem Biophys Rep Research Article Sortase A catalyzed ligation of ultra-short peptides leads to inter/intra-molecular transpeptidation to form either linear or cyclic oligomers dependent upon the peptide length. Cyclic peptides were the main products for peptides with more than 15aa. However, for ultra-short (<15aa) peptides, cyclic oligomers became predominant in prolonged reactions. Peptides with 1–3 aminoglycines were equally active but peptide oligomers from peptide containing more than one aminoglycine were prone to hydrolysis. Elsevier 2017-02-20 /pmc/articles/PMC5614665/ /pubmed/28955731 http://dx.doi.org/10.1016/j.bbrep.2017.02.005 Text en © 2017 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Voloshchuk, Natalya
Chen, Long
Li, Qiang
Liang, Jun F.
Peptide oligomers from ultra-short peptides using sortase
title Peptide oligomers from ultra-short peptides using sortase
title_full Peptide oligomers from ultra-short peptides using sortase
title_fullStr Peptide oligomers from ultra-short peptides using sortase
title_full_unstemmed Peptide oligomers from ultra-short peptides using sortase
title_short Peptide oligomers from ultra-short peptides using sortase
title_sort peptide oligomers from ultra-short peptides using sortase
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5614665/
https://www.ncbi.nlm.nih.gov/pubmed/28955731
http://dx.doi.org/10.1016/j.bbrep.2017.02.005
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