Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release

Yanfei Liu, Ling Zhang, Wei Wei Key Laboratory of Cell Engineering of Guizhou Province, Affiliated Hospital of Zunyi Medical College, Zunyi, Guizhou, People’s Republic of China Abstract: Peptide self-assembly is one of the promising bottom-up approaches for creating synthetic supermolecu...

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Autores principales:	Liu YF, Zhang L, Wei W
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2017
Materias:	peptide self-assembly hydrogel non-covalent interaction growth factor delivery proliferation signaling pathways Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/fc4b73c685e94e038d580f3974a50ba0
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spelling	oai:doaj.org-article:fc4b73c685e94e038d580f3974a50ba02021-12-02T07:36:51ZEffect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release1178-2013https://doaj.org/article/fc4b73c685e94e038d580f3974a50ba02017-01-01T00:00:00Zhttps://www.dovepress.com/effect-of-noncovalent-interaction-on-the-self-assembly-of-a-designed-p-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Yanfei Liu, Ling Zhang, Wei Wei Key Laboratory of Cell Engineering of Guizhou Province, Affiliated Hospital of Zunyi Medical College, Zunyi, Guizhou, People’s Republic of China Abstract: Peptide self-assembly is one of the promising bottom-up approaches for creating synthetic supermolecular architectures. Noncovalent interactions such as hydrophobic packing, electrostatic interaction, and polypeptide chain entropy (ΔSC) are the most relevant factors that affect the folding and self-assembly of peptides and the stability of supermolecular structures. The GVGV tetrapeptide is an abundant repeat in elastin, an extracellular matrix protein. In this study, four GVGV-containing peptides were designed with the aim of understanding the effects of these weak interactions on peptide self-assembly. Transmission electron microscopy, circular dichroism spectroscopy, dynamic light scattering measurements, and rheometry assays were used to study the structural features of the peptides. Because self-assembling peptides with different amino acid sequences may significantly affect protein release, basic fibroblast growth factor (bFGF) was used as a model molecule and encapsulated within the P2 (RLDLGVGVRLDLGVGV) hydrogel to study the release kinetics. The results showed that the balance among hydrophobic effects, electrostatic interactions, and chain entropy determined the molecular state and self-assembly of the peptide. Moreover, encapsulation of bFGF within the P2 hydrogel allowed its sustained release without causing changes in the secondary structure. The release profiles could be tuned by adjusting the P2 hydrogel concentration. Cell Counting Kit-8 and Western blot assays demonstrated that the encapsulated and released bFGFs were biologically active and capable of promoting the proliferation of murine fibroblast NIH-3T3 cells, most likely due to the activation of downstream signaling pathways. Keywords: peptide self-assembly, hydrogel, noncovalent interaction, growth factor delivery, proliferation, signaling pathwaysLiu YFZhang LWei WDove Medical Pressarticlepeptide self-assemblyhydrogelnon-covalent interactiongrowth factor deliveryproliferationsignaling pathwaysMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol Volume 12, Pp 659-670 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	peptide self-assembly hydrogel non-covalent interaction growth factor delivery proliferation signaling pathways Medicine (General) R5-920
spellingShingle	peptide self-assembly hydrogel non-covalent interaction growth factor delivery proliferation signaling pathways Medicine (General) R5-920 Liu YF Zhang L Wei W Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release
description	Yanfei Liu, Ling Zhang, Wei Wei Key Laboratory of Cell Engineering of Guizhou Province, Affiliated Hospital of Zunyi Medical College, Zunyi, Guizhou, People’s Republic of China Abstract: Peptide self-assembly is one of the promising bottom-up approaches for creating synthetic supermolecular architectures. Noncovalent interactions such as hydrophobic packing, electrostatic interaction, and polypeptide chain entropy (ΔSC) are the most relevant factors that affect the folding and self-assembly of peptides and the stability of supermolecular structures. The GVGV tetrapeptide is an abundant repeat in elastin, an extracellular matrix protein. In this study, four GVGV-containing peptides were designed with the aim of understanding the effects of these weak interactions on peptide self-assembly. Transmission electron microscopy, circular dichroism spectroscopy, dynamic light scattering measurements, and rheometry assays were used to study the structural features of the peptides. Because self-assembling peptides with different amino acid sequences may significantly affect protein release, basic fibroblast growth factor (bFGF) was used as a model molecule and encapsulated within the P2 (RLDLGVGVRLDLGVGV) hydrogel to study the release kinetics. The results showed that the balance among hydrophobic effects, electrostatic interactions, and chain entropy determined the molecular state and self-assembly of the peptide. Moreover, encapsulation of bFGF within the P2 hydrogel allowed its sustained release without causing changes in the secondary structure. The release profiles could be tuned by adjusting the P2 hydrogel concentration. Cell Counting Kit-8 and Western blot assays demonstrated that the encapsulated and released bFGFs were biologically active and capable of promoting the proliferation of murine fibroblast NIH-3T3 cells, most likely due to the activation of downstream signaling pathways. Keywords: peptide self-assembly, hydrogel, noncovalent interaction, growth factor delivery, proliferation, signaling pathways
format	article
author	Liu YF Zhang L Wei W
author_facet	Liu YF Zhang L Wei W
author_sort	Liu YF
title	Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release
title_short	Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release
title_full	Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release
title_fullStr	Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release
title_full_unstemmed	Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release
title_sort	effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bfgf release
publisher	Dove Medical Press
publishDate	2017
url	https://doaj.org/article/fc4b73c685e94e038d580f3974a50ba0
work_keys_str_mv	AT liuyf effectofnoncovalentinteractionontheselfassemblyofadesignedpeptideanditspotentialuseasacarrierforcontrolledbfgfrelease AT zhangl effectofnoncovalentinteractionontheselfassemblyofadesignedpeptideanditspotentialuseasacarrierforcontrolledbfgfrelease AT weiw effectofnoncovalentinteractionontheselfassemblyofadesignedpeptideanditspotentialuseasacarrierforcontrolledbfgfrelease
_version_	1718399378474926080

Effect of noncovalent interaction on the self-assembly of a designed peptide and its potential use as a carrier for controlled bFGF release

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