Engineering of an Extremely Thermostable Alpha/Beta Barrel Scaffold to Serve as a High Affinity Molecular Recognition Element for Use in Sensor Applications

Abstract

The overall goal of the project was to evolve a highly thermostable enzyme (alcohol dehydrogenase D (AdhD) from Pyrococcus furiosus) to bind an explosive molecule, RDX. The enzyme naturally catalyzes the nicotinamide cofactor-dependent oxidation or reduction of alcohols, aldehydes, ketones and carbohydrates. Directed evolution techniques were used to convert the enzyme into a simple binder of the small molecule RDX. Novel binders have been identified and characterized with sub-millimolar dissociation constants. These could be further developed for use in robust and low cost biosensors.

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Document Details

Document Type
Technical Report
Publication Date
Dec 23, 2015
Accession Number
AD1007471

Entities

People

  • Jennifer Haghpanah
  • Scott Banta

Organizations

  • Columbia University

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Amino Acids
  • Analytical Chemistry
  • Biomedical Engineering
  • Biosensors
  • Chemical Engineering
  • Chemical Synthesis
  • Chemistry
  • Department Of Defense
  • Engineering
  • Explosives Detection
  • Mathematics
  • Molecules
  • Protein Engineering
  • Small Molecules
  • Standards
  • Students
  • Thermostability

Fields of Study

  • Chemistry

Readers

  • Gulf War Illness and Chronic Multisymptom Illness in Veterans.
  • Molecular Genetics
  • Organic Chemistry

Technology Areas

  • Biotechnology