Collagen electrospun scaffolds potentially couple high biomimetism of the biological material with the fibrous morphology of the protein. However, there are conflicting reports in the literature addressing the presence of ultrastructure of collagen in electrospun fibers. In this work collagen type I fibers were obtained by electrospinning from two different solvents, trifluoroethanol (TFE) and dilute acetic acid (AcOH) and characterized by SEM, ATR-IR, Circular Dichroism and WAXD. We demonstrated that collagen electrospun fibers contained a very low amount of triple helix with respect to pristine collagen and that triple helix denaturation occurred during polymer dissolution. Collagen scaffolds were crosslinked for the first time by using 1,4-butanediol diglycidyl ether (BDDGE), in addition to the commonly employed 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) crosslinker. We proved that BDDGE is able to successfully crosslink collagen and preserve at the same time the scaffold fibrous morphology. Mesenchymal stem cell experiments demonstrated that collagen scaffolds crosslinked with BDDGE are biocompatible and support cell attachment.
Comparative performance of collagen nanofibers electrospun from different solvents and stabilized by different crosslinkers
GUALANDI, CHIARA;FIORANI, ANDREA;PANSERI, SILVIA;MONTESI, MONICA;MARCACCI, MAURILIO;FOCARETE, MARIA LETIZIA;BIGI, ADRIANA
2014
Abstract
Collagen electrospun scaffolds potentially couple high biomimetism of the biological material with the fibrous morphology of the protein. However, there are conflicting reports in the literature addressing the presence of ultrastructure of collagen in electrospun fibers. In this work collagen type I fibers were obtained by electrospinning from two different solvents, trifluoroethanol (TFE) and dilute acetic acid (AcOH) and characterized by SEM, ATR-IR, Circular Dichroism and WAXD. We demonstrated that collagen electrospun fibers contained a very low amount of triple helix with respect to pristine collagen and that triple helix denaturation occurred during polymer dissolution. Collagen scaffolds were crosslinked for the first time by using 1,4-butanediol diglycidyl ether (BDDGE), in addition to the commonly employed 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) crosslinker. We proved that BDDGE is able to successfully crosslink collagen and preserve at the same time the scaffold fibrous morphology. Mesenchymal stem cell experiments demonstrated that collagen scaffolds crosslinked with BDDGE are biocompatible and support cell attachment.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
