Title
Fibrin Association at Hybrid Biointerfaces Made of Clot-Binding Peptides and Polythiophene
Date Issued
01 October 2016
Access level
open access
Resource Type
journal article
Author(s)
Universitat Politècnica de Catalunya
Publisher(s)
Wiley-VCH Verlag
Abstract
The properties as biointerfaces of electroactive conducting polymer–peptide biocomposites formed by poly(3,4-ethylenedioxythiophene) (PEDOT) and CREKA or CR(NMe)EKA peptide sequences (where Glu has been replaced by N-methyl-Glu in the latter) have been compared. CREKA is a linear pentapeptide that recognizes clotted plasma proteins and selectively homes to tumors, while CR(NMe)EKA is an engineer to improve such properties by altering peptide–fibrin interactions. Differences between PEDOT-CREKA and PEDOT-CR(NMe)EKA reflect dissemblance in the organization of the peptides into the polymeric matrix. Both peptides affect fibrinogen thrombin-catalyzed polymerization causing the immediate formation of fibrin, whereas in the absence of thrombin this phenomenon is only observed for CR(NMe)EKA. Consistently, the fibrin-adsorption capacity is higher for PEDOT-CR(NMe)EKA than for PEDOT-CREKA, even though in both cases adsorbed fibrin exhibits round-like morphologies rather than the characteristic fibrous structure. PEDOT-peptide films coated with fibrin are selective in terms of cell adhesion, promoting the attachment of metastatic cells with respect to normal cells. (Figure presented.).
Start page
1461
End page
1474
Language
English
OCDE Knowledge area
Ingeniería química
Subjects
Scopus EID
2-s2.0-84990861351
PubMed ID
Source
Macromolecular Bioscience
ISSN of the container
16165187
Sources of information:
Directorio de Producción Científica
Scopus