replaced by an exotic amino acid bearing a 3,4-ethylenedioxythiophene ring in the side chain. The incorporation of the peptide at the end of preformed PEDOT chains has been corroborated by both FTIR and X-ray photoelectron spectroscopies. Although the morphology and topology are not influenced by the incorporation of the peptide to the end 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 bioactivies 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, results indicate that PEDOT promotes the exchange of ions at the conjugatecell interface.

The current experimental techniques of surfaces characterization provide structural information on a much larger scale than that in which atomistic details can be observed.In this work, this size gap gets reduced by consistently combining different modeling techniques that leads to describe the topographic profiles of thin polymer coatings at the atomistic level. A new modeling protocol, that combines Monte Carlo generation with Molecular Dynamics relaxation, has allowed us reproducing the experimental topography of extremely thin Poly(3,4-ethylenedioxythiophene) coating films using only the generated molecular models. The clue element of this protocol relies on parceling the studied surfaces in independent small plots, of which detailed molecular models are built. Combining a finite number of independent models enables to mimic the molecular organization of a large length of film that is orders of magnitude lager than the commonly used size in molecular models. The reconstructed area reproduces the thickness and roughness of very thin polymer coatings that were explicitly obtained for this study using very short electropolymerization times. This work shows a feasible way of visualizing with atomistic detail coated surfaces with polymeric films. ∑ − =1Where n m is the number added new RUs, is the probability weight of each combination of added RUs and β is (Tκ) -1 , where T is Temperature in K and κ the Boltzmann constant.

Outer-membrane porins are currently being used to prepare bioinspired nanomembranes for selective ion transport by immobilizing them into polymeric matrices. However, the fabrication of these protein-integrated devices has been found to be strongly influenced by the instability of the β-barrel porin structure, which depends on surrounding environment. In this work, molecular dynamics simulations have been used to investigate the structural stability of a representative porin, OmpF, in three different environments: (i) aqueous solution at pH=7; (ii) a solution of neutral detergent in a concentration similar to the critical micelle concentration; and (iii) the protein embedded into a neutral detergent bilayer. The results indicate that the surrounding environment not only alters the stability of the β-barrel but affects the internal loop responsible of the ions transport, as well as the tendency of the porin proteins to aggregate into trimers. The detergent bilayer preserves the structure of OmpF protein as is found bacteria membranes, while pure aqueous solution induces a strong destabilization of the protein. An intermediate situation occurs for detergent solution. Our results have been rationalized in terms of protein⋯water and protein⋯detergent interactions, which makes them extremely useful for the future design of new generation of bioinspired protein-integrated devices.