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oai:uvadoc.uva.es:10324/738642025-01-17T07:12:24Zcom_10324_1134com_10324_931com_10324_894col_10324_1213

Girotti ., Alessandra González Valdivieso, Juan Santos García, María Mercedes Martín Maroto, Laura Arias Vallejo, Francisco Javier 2025-01-15T10:51:55Z 2025-01-15T10:51:55Z 2020 International Journal of Biological Macromolecules, diciembre 2020, vol. 164, p. 1640-1648 0141-8130 https://uvadoc.uva.es/handle/10324/73864 10.1016/j.ijbiomac.2020.08.004 1640 1648 International Journal of Biological Macromolecules 164 One of the main goals in both tissue engineering and regenerative medicine is to design innovative synthetic scaffolds that can simulate and control the communication pathways between cells and the extracellular matrix (ECM). In this context, we describe herein the characterization of protein polymer, a recombinant elastin-like recombinamer (ELR) designed for developing tissue-engineered devices for use in vascular regeneration. This ELR is composed of an elastin-like backbone that contains a fibronectin domain, which provides specific, endothelial cell adhesion, and a protease target domain directed towards specific proteases involved in ECM remodeling. We also compare the specific response of endothelial and fibroblast cells to ELR scaffolds and show that cell adhesion and spreading on this ELR is significantly higher for endothelial cells than for fibroblasts. The reactivity of this polymer and its hydrogels to specific enzymatic degradation is demonstrated in vitro. As with natural elastin, enzymatic hydrolysis of the ELR produces elastin-derived peptides, or “matrikines”, which, in turn, are potentially able to regulate important cell activities. eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-nd/4.0/ © 2020 Published by Elsevier B.V. Attribution-NonCommercial-NoDerivatives 4.0 Internacional Functional characterization of an enzymatically degradable multi-bioactive elastin-like recombinamer info:eu-repo/semantics/article