{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["22(14)"],"submitter":["Ben Abla A"],"pubmed_abstract":["Engineering of biomimetic motives have emerged as promising approaches to improving cells' binding properties of biomaterials for tissue engineering and regenerative medicine. In this study, a bio-adhesive ligand including cell-binding domains of human fibronectin (FN) was engineered using recombinant protein technology, a major extracellular matrix (ECM) protein that interacts with a variety of integrins cell-surface's receptors and other ECM proteins through specific binding domains. 9th and 10th fibronectin type III repeat containing Arginine-Glycine-Aspartic acid (RGD) and Pro-His-Ser-Arg-Asn (PHSRN) synergic site (FNIII9-10) were expressed in fusion with a Colored Multi Affinity Tag (CMAT) to develop a simplified production and characterization process. A recombinant fragment was prod"],"journal":["International journal of molecular sciences"],"pagination":["7362"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8303147"],"repository":["biostudies-literature"],"pubmed_title":["Engineering of Bio-Adhesive Ligand Containing Recombinant RGD and PHSRN Fibronectin Cell-Binding Domains in Fusion with a Colored Multi Affinity Tag: Simple Approach for Fragment Study from Expression to Adsorption."],"pmcid":["PMC8303147"],"pubmed_authors":["Elmarjou A","Dridi C","Ben Abla A","Poirier F","Elm'selmi A","Boeuf G","Lutomski D","Changotade S"],"additional_accession":[]},"is_claimable":false,"name":"Engineering of Bio-Adhesive Ligand Containing Recombinant RGD and PHSRN Fibronectin Cell-Binding Domains in Fusion with a Colored Multi Affinity Tag: Simple Approach for Fragment Study from Expression to Adsorption.","description":"Engineering of biomimetic motives have emerged as promising approaches to improving cells' binding properties of biomaterials for tissue engineering and regenerative medicine. In this study, a bio-adhesive ligand including cell-binding domains of human fibronectin (FN) was engineered using recombinant protein technology, a major extracellular matrix (ECM) protein that interacts with a variety of integrins cell-surface's receptors and other ECM proteins through specific binding domains. 9th and 10th fibronectin type III repeat containing Arginine-Glycine-Aspartic acid (RGD) and Pro-His-Ser-Arg-Asn (PHSRN) synergic site (FNIII9-10) were expressed in fusion with a Colored Multi Affinity Tag (CMAT) to develop a simplified production and characterization process. A recombinant fragment was prod","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jul","modification":"2025-04-05T00:43:04.343Z","creation":"2022-02-11T00:10:55.795Z"},"accession":"S-EPMC8303147","cross_references":{"pubmed":["34298982"],"doi":["10.3390/ijms22147362"]}}