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Complexation of CXCL12, FGF-2 and VEGF with heparin modulates the protein release from alginate microbeads
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SYSNO ASEP 0547347 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Complexation of CXCL12, FGF-2 and VEGF with heparin modulates the protein release from alginate microbeads Author(s) Adrian, Edyta (UMCH-V) ORCID, RID
Treĺová, D. (SK)
Filová, Elena (FGU-C) RID, ORCID
Kumorek, Marta M. (UMCH-V) RID
Lobaz, Volodymyr (UMCH-V) RID, ORCID
Poreba, Rafal (UMCH-V) RID, ORCID
Janoušková, Olga (UMCH-V) RID, SAI, ORCID
Pop-Georgievski, Ognen (UMCH-V) RID, ORCID
Lacík, I. (SK)
Kubies, Dana (UMCH-V) RID, ORCIDArticle number 11666 Source Title International Journal of Molecular Sciences. - : MDPI
Roč. 22, č. 21 (2021)Number of pages 25 s. Language eng - English Country CH - Switzerland Keywords alginate microbeads ; heparin ; CXCL12 Subject RIV CD - Macromolecular Chemistry OECD category Polymer science Subject RIV - cooperation Institute of Physiology - Biotechnology ; Bionics R&D Projects NV16-28254A GA MZd - Ministry of Health (MZ) NV19-02-00068 GA MZd - Ministry of Health (MZ) GA20-08679S GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support UMCH-V - RVO:61389013 ; FGU-C - RVO:67985823 UT WOS 000718946200001 EID SCOPUS 85117956006 DOI 10.3390/ijms222111666 Annotation Long-term delivery of growth factors and immunomodulatory agents is highly required to support the integrity of tissue in engineering constructs, e.g., formation of vasculature, and to minimize immune response in a recipient. However, for proteins with a net positive charge at the physiological pH, controlled delivery from negatively charged alginate (Alg) platforms is challenging due to electrostatic interactions that can hamper the protein release. In order to regulate such interactions between proteins and the Alg matrix, we propose to complex proteins of interest in this study - CXCL12, FGF-2, VEGF - with polyanionic heparin prior to their encapsulation into Alg microbeads of high content of α-L-guluronic acid units (high-G). This strategy effectively reduced protein interactions with Alg (as shown by model ITC and SPR experiments) and, depending on the protein type, afforded control over the protein release for at least one month. The released proteins retained their in vitro bioactivity: CXCL12 stimulated the migration of Jurkat cells, and FGF-2 and VEGF induced proliferation and maturation of HUVECs. The presence of heparin also intensified protein biological efficiency. The proposed approach for encapsulation of proteins with a positive net charge into high-G Alg hydrogels is promising for controlled long-term protein delivery under in vivo conditions. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2022 Electronic address https://www.mdpi.com/1422-0067/22/21/11666
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