This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Add to Saved Citations Download to citation manager Request Permissions Request Reprints Add to My Marked Citations Citing Articles Citing Articles via Google Scholar Citing Articles via Scopus Google Scholar Articles by Santin, M. Articles by Motta, A. Search for Related Content Social Bookmarking                         What's this?

Domain-Driven Binding of Fibrin(Ogen) onto Silk Fibroin Biomaterials

Stephen P. Denyer

Andrew W. Lloyd

School of Pharmacy and Biomolecular Sciences, University of Brighton, Lewes Road, Brighton BN2 4GJ, UK

Antonella Motta

Department of Materials Engineering, University of Trento, Via Mesiano 77, 38050 Trento, Italy

Studies have demonstrated that serum protein adsorption onto silk fibroin-based biomaterials dramatically changes when the conformation of this natural polymer is rearranged by engineering procedures. In the present study, attention was paid to the binding of fibrin(ogen) to fibroin fibers and regenerated films. The fibroin specimens were incubated either in human plasma or in a fibrinogen solution to which thrombinwas added to activate the polymerization of the precursor into the final product, fibrin. The experiments were carried out in the presence and absence of calcium to investigate the role of calcium-dependent enzymes in the binding process. The two types of samples were analyzed by SEM, the micrographs showed completely different interactions with fibrinogen. Films did not show any visible fibrin polymerization, whereas the fibers were bound to the fibrin bundles by calcium-independent mechanisms.

Journal of Bioactive and Compatible Polymers, Vol. 17, No. 3, 195-208 (2002)
DOI: 10.1106/088391102026326


CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?