2026-04-17T05:43:50Zhttps://recercat.cat/oai/request

oai:recercat.cat:2117/1042652026-02-07T08:59:27Zcom_2072_1033col_2072_452950

00925njm 22002777a 4500 dc Triguero Enguídanos, Jordi author Zanuy Gomara, David author Alemán Llansó, Carlos author 2017-02-01 The conformational preferences of the Arg-GlE-Asp sequence, where GlE is an engineered amino acid bearing a 3,4-ethylenedioxythiophene (EDOT) ring as side group, have been determined combining density functional theory calculations with a well-established conformational search strategy. Although the Arg-GlE-Asp sequence was designed to prepare a conducting polymer–peptide conjugate with excellent electrochemical and bioadhesive properties, the behavior of such hybrid material as adhesive biointerface is improvable. Results obtained in this work prove that the bioactive characteristics of the parent Arg-Gly-Asp sequence become unstable in Arg-GlE-Asp because of both the steric hindrance caused by the EDOT side group and the repulsive interactions between the oxygen atoms belonging to the backbone amide groups and the EDOT side group. Detailed analyses of the conformational preferences identified in this work have been used to re-engineer the Arg-GlE-Asp sequence for the future development of a new electroactive conjugate with improved bioadhesive properties. The preparation of this new conjugate is in progress. Peer Reviewed Postprint (author's final draft) Àrees temàtiques de la UPC::Enginyeria química Peptides Polymers in medicine adhesive peptides bioactive conformation conformational search conjugate 3 4-ethylenedioxythiophene molecular engineering polymer-peptide Biopolímers Pèptids Adhesius Conformational analysis of a modified RGD adhesive sequence