Towards an experimental classification system for membrane active peptides

Abstract Mature proteins can act as potential sources of encrypted bioactive peptides that, once released from their parent proteins, might interact with diverse biomolecular targets. In recent work we introduced a systematic methodology to uncover encrypted intragenic antimicrobial peptides (IAPs)...

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Autores principales:	G. D. Brand, M. H. S. Ramada, T. C. Genaro-Mattos, C. Bloch
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2154bb41ee184745bb7ea43f16962c15
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spelling	oai:doaj.org-article:2154bb41ee184745bb7ea43f16962c152021-12-02T15:08:22ZTowards an experimental classification system for membrane active peptides10.1038/s41598-018-19566-w2045-2322https://doaj.org/article/2154bb41ee184745bb7ea43f16962c152018-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-19566-whttps://doaj.org/toc/2045-2322Abstract Mature proteins can act as potential sources of encrypted bioactive peptides that, once released from their parent proteins, might interact with diverse biomolecular targets. In recent work we introduced a systematic methodology to uncover encrypted intragenic antimicrobial peptides (IAPs) within large protein sequence libraries. Given that such peptides may interact with membranes in different ways, resulting in distinct observable outcomes, it is desirable to develop a predictive methodology to categorize membrane active peptides and establish a link to their physicochemical properties. Building upon previous work, we explored the interaction of a range of IAPs with model membranes probed by differential scanning calorimetry (DSC) and circular dichroism (CD) techniques. The biophysical data were submitted to multivariate statistical methods and resulting peptide clusters were correlated to peptide structure and to their antimicrobial activity. A re-evaluation of the physicochemical properties of the peptides was conducted based on peptide cluster memberships. Our data indicate that membranolytic peptides produce characteristic thermal transition (DSC) profiles in model vesicles and that this can be used to categorize novel molecules with unknown biological activity. Incremental expansion of the model presented here might result in a unified experimental framework for the prediction of novel classes of membrane active peptides.G. D. BrandM. H. S. RamadaT. C. Genaro-MattosC. BlochNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q G. D. Brand M. H. S. Ramada T. C. Genaro-Mattos C. Bloch Towards an experimental classification system for membrane active peptides
description	Abstract Mature proteins can act as potential sources of encrypted bioactive peptides that, once released from their parent proteins, might interact with diverse biomolecular targets. In recent work we introduced a systematic methodology to uncover encrypted intragenic antimicrobial peptides (IAPs) within large protein sequence libraries. Given that such peptides may interact with membranes in different ways, resulting in distinct observable outcomes, it is desirable to develop a predictive methodology to categorize membrane active peptides and establish a link to their physicochemical properties. Building upon previous work, we explored the interaction of a range of IAPs with model membranes probed by differential scanning calorimetry (DSC) and circular dichroism (CD) techniques. The biophysical data were submitted to multivariate statistical methods and resulting peptide clusters were correlated to peptide structure and to their antimicrobial activity. A re-evaluation of the physicochemical properties of the peptides was conducted based on peptide cluster memberships. Our data indicate that membranolytic peptides produce characteristic thermal transition (DSC) profiles in model vesicles and that this can be used to categorize novel molecules with unknown biological activity. Incremental expansion of the model presented here might result in a unified experimental framework for the prediction of novel classes of membrane active peptides.
format	article
author	G. D. Brand M. H. S. Ramada T. C. Genaro-Mattos C. Bloch
author_facet	G. D. Brand M. H. S. Ramada T. C. Genaro-Mattos C. Bloch
author_sort	G. D. Brand
title	Towards an experimental classification system for membrane active peptides
title_short	Towards an experimental classification system for membrane active peptides
title_full	Towards an experimental classification system for membrane active peptides
title_fullStr	Towards an experimental classification system for membrane active peptides
title_full_unstemmed	Towards an experimental classification system for membrane active peptides
title_sort	towards an experimental classification system for membrane active peptides
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/2154bb41ee184745bb7ea43f16962c15
work_keys_str_mv	AT gdbrand towardsanexperimentalclassificationsystemformembraneactivepeptides AT mhsramada towardsanexperimentalclassificationsystemformembraneactivepeptides AT tcgenaromattos towardsanexperimentalclassificationsystemformembraneactivepeptides AT cbloch towardsanexperimentalclassificationsystemformembraneactivepeptides
_version_	1718388172978651136

Towards an experimental classification system for membrane active peptides

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