Biomolecular Films (Surfactant Science Series) by James F. Rusling

By James F. Rusling

Surveying specific and smooth biomolecular movie methodologies and investigative suggestions, this article examines motion pictures of biomolecules which could offer strong surfaces for catalyzing enzyme reactions, serve in biosensors and as biorecognition parts, mediate nanoparticle formation, and supply a foundation for basic reports and functions in biomedicine and biomedical units. The authors speak about designing practical biomolecular motion pictures on electrodes, biomimetic membranes on steel helps, peptide and protein-based biomolecular assemblies, floor plasmon resonance spectroscopy, and biosensors.

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Enzymes can be bound on the surface, partly inserted, or extend fully across the biomembrane (Fig. 13). Biomembrane-like structures of lipids or insoluble synthetic surfactants containing proteins have been constructed on electrodes in a number of ways. To mimic biological membranes, lipids or surfactants should reside on the electrode in bilayer structures such as in Fig. 13. Below, we brie£y review structural characteristics that cause lipid and surfactant molecules to form bilayers. Designing Functional Biomolecular Films 33 FIG.

5 mm after soaking in bu¡er for about 1 h, but then remain stable for weeks. This may occur because phosphatidylcholines are slightly more water-soluble that the very insoluble DDAB. Midpoint potentials of the CVs of MbÀlipid and cyt P450camÀlipid ¢lms shifted negative with increasing solution pH. The properties of the proteins in these ¢lms are controlled by the pH and salt content of the external solution. Mb gave direct, reversible heme FeIII=FeII electron transfer in a variety of ¢lms of double-chain or triple-chain surfactants [64,156] on PG, Au, ITO, or Pt electrodes.

75 V. At this potential, phosphate adsorbs to HOPG and may facilitate the reversible electrochemistry [94]. An AFM-electrochemical study of Cys3Ser azurin on gold showed an electroinactive ¢lm of protein also featuring two-dimensional aggregates [96]. Cys3Ser azurin ¢lms gave an unstable, decaying redox peak on edge-plane pyrolytic graphite. Thus, direct adsorption of proteins on conductive (nonoxide) electrode surfaces can give electroactive ¢lms, but may result in problems with protein aggregation and limited stability.

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