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Fibrin Association at Hybrid Biointerfaces Made of Clot‐Binding Peptides and Polythiophene
Author(s) -
PuiggalíJou A.,
del Valle Luis J.,
Armelin Elaine,
Alemán Carlos
Publication year - 2016
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201600128
Subject(s) - fibrin , chemistry , pedot:pss , thrombin , peptide , fibrinogen , polymerization , conductive polymer , biophysics , polymer chemistry , polymer , biochemistry , organic chemistry , platelet , immunology , biology
The properties as biointerfaces of electroactive conducting polymer–peptide biocomposites formed by poly(3,4‐ethylenedioxythiophene) (PEDOT) and CREKA or CR( N Me)EKA peptide sequences (where Glu has been replaced by N ‐methyl‐Glu in the latter) have been compared.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( N Me)EKA is an engineer to improve such properties by altering peptide–fibrin interactions. Differences between PEDOT‐CREKA and PEDOT‐CR( N Me)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( N Me)EKA. Consistently, the fibrin‐adsorption capacity is higher for PEDOT‐CR( N Me)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.