title: Electroactive polymer-peptide conjugates for adhesive biointerfaces.
abstract: Electroactive polymer-peptide conjugates have been synthesized by combining poly(3,4-ethylenedioxythiophene), a polythiophene derivative with outstanding properties, and an Arg-Gly-Asp (RGD)-based peptide in which Gly has been replaced by an exotic amino acid bearing a 3,4-ethylenedioxythiophene ring in the side chain. The incorporation of the peptide at the ends of preformed PEDOT chains has been corroborated by both FTIR and X-ray photoelectron spectroscopy. Although the morphology and topology are not influenced by the incorporation of the peptide at the ends of PEDOT chains, this process largely affects other surface properties. Thus, the wettability of the conjugates is considerably higher than that of PEDOT, independently of the synthetic strategy, whereas the surface roughness only increases when the conjugate is obtained using a competing strategy (i.e. growth of the polymer chains against termination by end capping). The electrochemical activity of the conjugates has been found to be higher than that of PEDOT, evidencing the success of the polymer-peptide links designed by chemical similarity. Density functional theory calculations have been used not only to ascertain the conformational preferences of the peptide but also to interpret the electronic transitions detected by UV-vis spectroscopy. Electroactive surfaces prepared using the conjugates displayed the higher bioactivities in terms of cell adhesion, with the relative viabilities being dependent on the roughness, wettability and electrochemical activity of the conjugate. In addition to the influence of the peptide fragment in the initial cell attachment and subsequent cell spreading and survival, the results indicate that PEDOT promotes the exchange of ions at the conjugate-cell interface.
authors.affiliation: Departament d'Enginyeria Química, E. T. S. d'Enginyeria Industrial de Barcelona, Universitat Politècnica de Catalunya, Diagonal 647, 08028 Barcelona, Spain. carlos.aleman@upc.edu.
authors.forename: Silvana
authors.initials: S
authors.lastname: Maione
authors.forename: Ana M
authors.initials: AM
authors.lastname: Gil
authors.forename: Georgina
authors.initials: G
authors.lastname: Fabregat
authors.forename: Luis J
authors.initials: LJ
authors.lastname: Del Valle
authors.forename: Jordi
authors.initials: J
authors.lastname: Triguero
authors.forename: Adele
authors.initials: A
authors.lastname: Laurent
authors.forename: Denis
authors.initials: D
authors.lastname: Jacquemin
authors.forename: Francesc
authors.initials: F
authors.lastname: Estrany
authors.forename: Ana I
authors.initials: AI
authors.lastname: Jiménez
authors.forename: David
authors.initials: D
authors.lastname: Zanuy
authors.forename: Carlos
authors.initials: C
authors.lastname: Cativiela
authors.forename: Carlos
authors.initials: C
authors.lastname: Alemán
mesh_terms: D000269:Adhesives; D001672:Biocompatible Materials / Q000737:chemistry*; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000737:chemistry* / Q000378:metabolism; D002448:Cell Adhesion; D007477:Ions / Q000737:chemistry*; D008855:Microscopy, Electron, Scanning; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D056951:Photoelectron Spectroscopy; D011108:Polymers / Q000737:chemistry* / Q000378:metabolism; D013499:Surface Properties; D013876:Thiophenes / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000269:Adhesives; D001672:Biocompatible Materials; D019086:Bridged Bicyclo Compounds, Heterocyclic; D007477:Ions; D009842:Oligopeptides; D010446:Peptide Fragments; D010455:Peptides; D011108:Polymers; D013876:Thiophenes; C121383:poly(3,4-ethylene dioxythiophene); C066730:polythiophene; C047981:arginyl-glycyl-aspartic acid