{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shpichka AI"],"funding":["Russian Foundation for Basic Research","Russian Science Foundation"],"pagination":["4190-4200"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9049040"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(8)"],"pubmed_abstract":["Fibrin is a well-known tool in tissue engineering, but the structure of its modifications created to improve its properties remains undiscussed despite its importance, <i>e.g.</i> in designing biomaterials that ensure cell migration and lumenogenesis. We sought to uncover the structural aspects of PEGylated fibrin hydrogels shown to contribute to angiogenesis. The analysis of the small-angle X-ray scattering (SAXS) data and <i>ab initio</i> modeling revealed that the PEGylation of fibrinogen led to the formation of oligomeric species, which are larger at a higher PEG : fibrinogen molar ratio. The improvement of optical properties was provided by the decrease in aggregates' sizes and also by retaining the bound water. Compared to the native fibrin, the structure of the 5 : 1 PEGylated fibri"],"journal":["RSC advances"],"pubmed_title":["Digging deeper: structural background of PEGylated fibrin gels in cell migration and lumenogenesis."],"pmcid":["PMC9049040"],"funding_grant_id":["18-02-00658","17-02-00445","18-15-00407"],"pubmed_authors":["Konarev PV","Kosheleva NV","Shpichka AI","Zhigalina OM","Frolova AA","Volkov VV","Efremov YM","Aksenova NA","Kryukova AE","Kotova SL","Khmelenin DN","Yusupov VI","Koroleva A","Timashev PS","Asadchikov VE"],"additional_accession":[]},"is_claimable":false,"name":"Digging deeper: structural background of PEGylated fibrin gels in cell migration and lumenogenesis.","description":"Fibrin is a well-known tool in tissue engineering, but the structure of its modifications created to improve its properties remains undiscussed despite its importance, <i>e.g.</i> in designing biomaterials that ensure cell migration and lumenogenesis. We sought to uncover the structural aspects of PEGylated fibrin hydrogels shown to contribute to angiogenesis. The analysis of the small-angle X-ray scattering (SAXS) data and <i>ab initio</i> modeling revealed that the PEGylation of fibrinogen led to the formation of oligomeric species, which are larger at a higher PEG : fibrinogen molar ratio. The improvement of optical properties was provided by the decrease in aggregates' sizes and also by retaining the bound water. Compared to the native fibrin, the structure of the 5 : 1 PEGylated fibri","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jan","modification":"2025-04-21T16:47:35.288Z","creation":"2025-04-21T16:47:35.288Z"},"accession":"S-EPMC9049040","cross_references":{"pubmed":["35495227"],"doi":["10.1039/c9ra08169k"]}}