Presentation + Paper
21 August 2015 Modified kinetics of enzymes interacting with nanoparticles
Author Affiliations +
Abstract
Enzymes are important players in multiple applications, be it bioremediation, biosynthesis, or as reporters. The business of catalysis and inhibition of enzymes is a multibillion dollar industry and understanding the kinetics of commercial enzymes can have a large impact on how these systems are optimized. Recent advances in nanotechnology have opened up the field of nanoparticle (NP) and enzyme conjugates and two principal architectures for NP conjugate systems have been developed. In the first example the enzyme is bound to the NP in a persistent manner, here we find that key factors such as directed enzyme conjugation allow for enhanced kinetics. Through controlled comparative experiments we begin to tease out specific mechanisms that may account for the enhancement. The second system is based on dynamic interactions of the enzymes with the NP. The enzyme substrate is bound to the NP and the enzyme is free in solution. Here again we find that there are many variables , such as substrate positioning and NP selection, that modify the kinetics.
Conference Presentation
© (2015) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Sebastián A. Díaz, Joyce C. Breger, Anthony Malanoski, Jonathan C. Claussen, Scott A. Walper, Mario G. Ancona, Carl W. Brown III, Michael H. Stewart, Eunkeu Oh, Kimihiro Susumu, and Igor L. Medintz "Modified kinetics of enzymes interacting with nanoparticles", Proc. SPIE 9550, Biosensing and Nanomedicine VIII, 95500K (21 August 2015); https://doi.org/10.1117/12.2188212
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CITATIONS
Cited by 2 scholarly publications.
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KEYWORDS
Nanoparticles

Sensors

Fluorescence resonance energy transfer

Neptunium

Luminescence

Molecules

Calibration

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