Kinetics And Molecular Binding Of Gepis On Solid Surfaces.

Overview

Peptides biocombinatorially selected to bind to specific inorganic surfaces have been widely studied for their ability to bind to metal, oxide, mineral, and semiconducting surfaces. These genetically engineered peptides for inorganics (GEPIs) have attracted particular interest due to their applications as molecular linkers, surface modifiers, synthesizers of inorganic material and self-assembled platforms for nanostructures. While many studies using GEPIs have been conducted, there is still a general lack of ...
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Overview

Peptides biocombinatorially selected to bind to specific inorganic surfaces have been widely studied for their ability to bind to metal, oxide, mineral, and semiconducting surfaces. These genetically engineered peptides for inorganics (GEPIs) have attracted particular interest due to their applications as molecular linkers, surface modifiers, synthesizers of inorganic material and self-assembled platforms for nanostructures. While many studies using GEPIs have been conducted, there is still a general lack of understanding of their behavior in different applications and environments. Here, the interactions of GEPIs with inorganic surfaces are quantitatively characterized using real-time biosensing techniques, namely surface plasmon resonance spectroscopy (SPR) and quartz-crystal microbalance (QCM). In order to perform this study, a standard SPR setup was modified in order to allow the use of SPR analysis on surfaces other than gold. Using this technique, the binding kinetics of dozens of peptide sequences, including gold, silver, platinum, titanium, hydroxyapatite, quartz, and graphite binders, were characterized on multiple surfaces. Key results indicate the generally observed ability of peptides sequences to bind to the original surface used during the selection procedure, the determination of the effect of changes in conformation on the kinetics peptide binding, and the identification certain peptides that show a high degree of specificity to particular surfaces, showing low or no binding on other surfaces. The GEPIs tested in varying buffer conditions showed an ability to bind in a wide range of pHs, temperatures, and ionic strengths. In general, however, the binding isotherms observed were very poorly fit by common binding models. Analytical rate equation models were developed and employed to determine the importance of certain mechanisms in the observed molecular binding behavior. Finally, GEPIs were quantitatively tested for their kinetics in a number of proof-of-concept applications. In an enzyme immobilization study, for example enzymes immobilized via GEPIs showed significantly higher activity than those nonspecifically immobilized. In biomineralization studies, several bifunctional GEPIs showed the ability to mineralize hydroxyapatite out of a calcium phosphate solution, where control surfaces and peptides showed no mineralization ability.

With the present first study, which established quantitative molecular binding procedures of solid binding peptides, it is now possible to design, tailor and implement GEPIs for a wide range of applications, from nanotechnology to medical problems that require an interface between a biopolymer/biosurface and an inorganic surface.

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Product Details

  • ISBN-13: 9781244601109
  • Publisher: BiblioLabsII
  • Publication date: 9/30/2011
  • Pages: 244
  • Product dimensions: 7.44 (w) x 9.69 (h) x 0.51 (d)

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