Organophosphorus Surface Chemistry in Organized Media
Abstract
Principal objective was to understand the molecular interactions between organophosphates and the enzymes that are inhibited by organophosphates or enzymes that catalyze the hydrolysis of organophosphates, at the air/water interface (Langmuir films) and in Langmuir-Blodgett (L-B) films and to develop a biosensor with greater sensitivity. This report contains the data on detailed study of acetylcholinesterase (AChE) Langmuir films and molecular interactions between AChE and OP compounds in monolayers and in Langmuir-Blodgett films. Data demonstrates that acetylcholinesterase forms a highly stable monolayer at the air/aqueous interface. Brewster angle microscopy data indicate the reversible formation of domains upon compression and decompression of the enzyme monolayer at the air/aqueous interface. The tapping mode atomic force microscopy (TMAFM) data on L-B films of AChE indicate abundant globular AChE monomers and a limited number of large and medium sized tetramer forms of AChE. The TMAFM images and UV-vis and FTIR spectroscopic data suggest that the configuration of the enzyme was completely modified in the presence of the paraoxon and the ellipsoidal shape of AChE disappeared. As a continuation of this project, work was initiated on designing and testing of a biosensor using fluorescence labeled AChE monolayers and on characterization of Langmuir and Langmuir-Blodgett films of organophosphorus acid hydrolase and its interactions with organophosphorus compounds.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 2000
- Accession Number
- ADA384296
Entities
People
- Roger M. Leblanc
Organizations
- University of Miami