Acetylcholinesterase immobilized on modified magne... - BV FAPESP
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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Acetylcholinesterase immobilized on modified magnetic beads as a tool for screening a compound library

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Author(s):
Vanzolini, Kenia L. [1] ; Vieira, Lucas C. C. [1] ; Correa, Arlene. G. [1] ; Moaddel, Ruin [2] ; Cass, Quezia B. [1]
Total Authors: 5
Affiliation:
[1] Univ Fed Sao Carlos, Dept Quim, SEPARARE Nucleo Pesquisa Cromatog, BR-13565905 Sao Carlos, SP - Brazil
[2] NIA, Biomed Res Ctr, NIH, Baltimore, MD 21224 - USA
Total Affiliations: 2
Document type: Journal article
Source: Microchimica Acta; v. 182, n. 13-14, p. 2209-2213, OCT 2015.
Web of Science Citations: 8
Abstract

Acetylcholinesterase (AChE) from Electrophorus electricus was immobilized on the surface of amino-modified magnetic beads (AChE-MB), and its activity evaluated by the quantification of acetylcholine hydrolysis. A reference mixture composed of AChE binders (galanthamine and a probe coumarin, K (i) = 0.031 +/- 0.010 mu M) and non-binders (ketamine and propranolol) was used to probe the fishing assay. The performance of the bioconjugation assay was demonstrated with a library of 12 reference coumarins from which two ligands were directly identified by LC-MS/MS in a single assay, demonstrating the usefulness of this approach. (AU)

FAPESP's process: 13/02054-0 - Enzyme immobilization: new tools for ligand screening
Grantee:Kenia Lourenço Vanzolini
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 13/01710-1 - Enzyme ligand: new models of screening
Grantee:Quezia Bezerra Cass
Support Opportunities: Research Projects - Thematic Grants