000070770 001__ 70770
000070770 005__ 20180523160640.0
000070770 0247_ $$2doi$$a10.1107/S2052252515007538
000070770 0248_ $$2sideral$$a92030
000070770 037__ $$aART-2015-92030
000070770 041__ $$aeng
000070770 100__ $$aMacchi, P.
000070770 245__ $$aModelling the experimental electron density: Only the synergy of various approaches can tackle the new challenges
000070770 260__ $$c2015
000070770 5060_ $$aAccess copy available to the general public$$fUnrestricted
000070770 5203_ $$aElectroactive 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a polythiophene derivative with outstanding properties, and an Arg-Gly-Asp (RGD)-based peptide in which Gly has been replaced by an exotic amino acid bearing a 3,4-ethylenedioxythiophene ring in the side chain.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.
000070770 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E40$$9info:eu-repo/grantAgreement/ES/MINECO/MAT2012-34498
000070770 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000070770 590__ $$a3.105$$b2015
000070770 591__ $$aCRYSTALLOGRAPHY$$b5 / 26 = 0.192$$c2015$$dQ1$$eT1
000070770 591__ $$aMATERIALS SCIENCE, MULTIDISCIPLINARY$$b57 / 270 = 0.211$$c2015$$dQ1$$eT1
000070770 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b53 / 162 = 0.327$$c2015$$dQ2$$eT1
000070770 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000070770 700__ $$aGillet, J. -M
000070770 700__ $$aTaulelle, F.
000070770 700__ $$0(orcid)0000-0002-3600-1721$$aCampo, J.$$uUniversidad de Zaragoza
000070770 700__ $$aClaiser, N.
000070770 700__ $$aLecomte, C.
000070770 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDepartamento de Física de la Materia Condensada$$cFísica de la Materia Condensada
000070770 773__ $$g2, 4 (2015), 441-451$$pIUCrJ$$tIUCrJ$$x2052-2525
000070770 8564_ $$s476617$$uhttp://zaguan.unizar.es/record/70770/files/texto_completo.pdf$$yVersión publicada
000070770 8564_ $$s102747$$uhttp://zaguan.unizar.es/record/70770/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000070770 909CO $$ooai:zaguan.unizar.es:70770$$particulos$$pdriver
000070770 951__ $$a2018-05-23-14:56:55
000070770 980__ $$aARTICLE