Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers

Rajesh Vasita, Dhirendra S KattiDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, Uttar Pradesh, IndiaBackground: Hydrophobic biopolymers such as polylactide-co-glycolide (PLGA, 85:15) have been extensively explored as scaffolding materials for tissue engi...

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Autores principales:	Vasita R, Katti DS
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2011
Materias:	Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/a7eaea9fa5e8494f86ae45490c64fe71
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spelling	oai:doaj.org-article:a7eaea9fa5e8494f86ae45490c64fe712021-12-02T02:42:34ZStructural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers1176-91141178-2013https://doaj.org/article/a7eaea9fa5e8494f86ae45490c64fe712011-12-01T00:00:00Zhttp://www.dovepress.com/structural-and-functional-characterization-of-proteins-adsorbed-on-hyd-a8984https://doaj.org/toc/1176-9114https://doaj.org/toc/1178-2013Rajesh Vasita, Dhirendra S KattiDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, Uttar Pradesh, IndiaBackground: Hydrophobic biopolymers such as polylactide-co-glycolide (PLGA, 85:15) have been extensively explored as scaffolding materials for tissue engineering applications. More recently, electrospun microfiber-based and nanofiber-based scaffolds of PLGA have received increased attention because they act as physical mimics of the fibrillar extracellular matrix. However, the hydrophobicity of the PLGA microfiber surface can limit its use in biomedical applications. Therefore, in a previous study, we fabricated Pluronic&reg; F-108 (PF-108)-blended PLGA microfibrous scaffolds that alleviated the hydrophobicity associated with PLGA by enriching the surface of microfibers with the ethylene oxide units present in PF-108.Methods: In this study, we report the influence of the extent of surface enrichment of PLGA microfibers on their interaction with two model proteins, ie, bovine serum albumin (BSA) and lysozyme. BSA and lysozyme were adsorbed onto PLGA microfiber meshes (unmodified and modified) and studied for the amount, secondary structure conformation, and bioactivity of released protein.Results: Irrespective of the type of protein, PF-108-blended PLGA microfibers showed significantly greater protein adsorption and release than the unblended PLGA samples. However, in comparison with BSA, lysozyme showed a 7&ndash;9-fold increase in release. The Fourier transform infrared spectroscopy studies for secondary structure determination demonstrated that irrespective of type of microfiber surface (unblended or blended), adsorbed BSA and lysozyme did not show any significant change in secondary structure (&alpha;-helical content) as compared with BSA and/or lysozyme in the free powder state. Further, the bioactivity assay of lysozyme released from blended PLGA microfiber meshes demonstrated 80%&ndash;85% bioactivity, indicating that the process of adsorption did not significantly affect biological activity. Therefore, this study demonstrated that the decreased hydrophobicity of blended PLGA microfibrous meshes not only improved the amount of protein adsorbed (lysozyme and BSA) but also maintained the secondary structure and bioactivity of the adsorbed proteins.Conclusion: Modulating the hydrophobicity of PLGA via blending with PF-108 could be a viable strategy to improve its interaction with proteins and subsequent cell interaction in tissue engineering applications.Keywords: microfiber, protein adsorption, electrospinningVasita RKatti DSDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2012, Iss default, Pp 61-71 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine (General) R5-920
spellingShingle	Medicine (General) R5-920 Vasita R Katti DS Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
description	Rajesh Vasita, Dhirendra S KattiDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur, Uttar Pradesh, IndiaBackground: Hydrophobic biopolymers such as polylactide-co-glycolide (PLGA, 85:15) have been extensively explored as scaffolding materials for tissue engineering applications. More recently, electrospun microfiber-based and nanofiber-based scaffolds of PLGA have received increased attention because they act as physical mimics of the fibrillar extracellular matrix. However, the hydrophobicity of the PLGA microfiber surface can limit its use in biomedical applications. Therefore, in a previous study, we fabricated Pluronic&reg; F-108 (PF-108)-blended PLGA microfibrous scaffolds that alleviated the hydrophobicity associated with PLGA by enriching the surface of microfibers with the ethylene oxide units present in PF-108.Methods: In this study, we report the influence of the extent of surface enrichment of PLGA microfibers on their interaction with two model proteins, ie, bovine serum albumin (BSA) and lysozyme. BSA and lysozyme were adsorbed onto PLGA microfiber meshes (unmodified and modified) and studied for the amount, secondary structure conformation, and bioactivity of released protein.Results: Irrespective of the type of protein, PF-108-blended PLGA microfibers showed significantly greater protein adsorption and release than the unblended PLGA samples. However, in comparison with BSA, lysozyme showed a 7&ndash;9-fold increase in release. The Fourier transform infrared spectroscopy studies for secondary structure determination demonstrated that irrespective of type of microfiber surface (unblended or blended), adsorbed BSA and lysozyme did not show any significant change in secondary structure (&alpha;-helical content) as compared with BSA and/or lysozyme in the free powder state. Further, the bioactivity assay of lysozyme released from blended PLGA microfiber meshes demonstrated 80%&ndash;85% bioactivity, indicating that the process of adsorption did not significantly affect biological activity. Therefore, this study demonstrated that the decreased hydrophobicity of blended PLGA microfibrous meshes not only improved the amount of protein adsorbed (lysozyme and BSA) but also maintained the secondary structure and bioactivity of the adsorbed proteins.Conclusion: Modulating the hydrophobicity of PLGA via blending with PF-108 could be a viable strategy to improve its interaction with proteins and subsequent cell interaction in tissue engineering applications.Keywords: microfiber, protein adsorption, electrospinning
format	article
author	Vasita R Katti DS
author_facet	Vasita R Katti DS
author_sort	Vasita R
title	Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
title_short	Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
title_full	Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
title_fullStr	Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
title_full_unstemmed	Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
title_sort	structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers
publisher	Dove Medical Press
publishDate	2011
url	https://doaj.org/article/a7eaea9fa5e8494f86ae45490c64fe71
work_keys_str_mv	AT vasitar structuralandfunctionalcharacterizationofproteinsadsorbedonhydrophilizedpolylactidecoglycolidemicrofibers AT kattids structuralandfunctionalcharacterizationofproteinsadsorbedonhydrophilizedpolylactidecoglycolidemicrofibers
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Structural and functional characterization of proteins adsorbed on hydrophilized polylactide-co-glycolide microfibers

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