PERFORM Publications

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Title		Authors	PubMed ID
1	The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB	Bin X; Pawelek PD;	40400396 CHEMBIOCHEM
2	Evidence of isochorismate channeling between the Escherichia coli enterobactin biosynthetic enzymes EntC and EntB	Bin X; Pawelek PD;	39031458 CHEMBIOCHEM
3	New Megastigmane and Polyphenolic Components of Henna Leaves and Their Tumor-Specific Cytotoxicity on Human Oral Squamous Carcinoma Cell Lines	Orabi MAA; Orabi EA; Awadh AAA; Alshahrani MM; Abdel-Wahab BA; Sakagami H; Hatano T;	38001804 CHEMBIOCHEM
4	Structural determination and anticholinesterase assay of C-glycosidic ellagitannins from Lawsonia inermis leaves: A study supported by DFT calculations and molecular docking	Orabi MAA; Orabi EA; Abdel-Sattar ES; English AM; Hatano T; Elimam H;	36423882 CHEMBIOCHEM
5	Evidence of an intracellular interaction between the Escherichia coli enzymes EntC and EntB and identification of a potential electrostatic channeling surface	Ouellette S; Pakarian P; Bin X; Pawelek PD;	35952947 CHEMBIOCHEM
6	Identifying potential drug targets and candidate drugs for COVID-19: biological networks and structural modeling approaches	Selvaraj G; Kaliamurthi S; Peslherbe GH; Wei DQ;	33968364 CERMM
7	Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from Angelica decursiva.	Ali MY, Seong SH, Jung HA, Choi JS	31683604 CHEMBIOCHEM
8	Umbelliferone derivatives exert neuroprotective effects by inhibiting monoamine oxidase A, self-amyloidβ aggregation, and lipid peroxidation.	Seong SH, Ali MY, Jung HA, Choi JS	31557622 CHEMBIOCHEM
9	Virtual screening, docking, and dynamics of potential new inhibitors of dihydrofolate reductase from Yersinia pestis.	Bastos Lda C, de Souza FR, Guimarães AP, Sirouspour M, Cuya Guizado TR, Forgione P, Ramalho TC, França TC	26494420 CHEMISTRY
10	Mechanistic studies of new oximes reactivators of human butyryl cholinesterase inhibited by cyclosarin and sarin.	de Lima WE, Francisco A, da Cunha EF, Radic Z, Taylor P, França TC, Ramalho TC	27125569 CHEMISTRY
11	Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway.	Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS	31194956 BIOLOGY

Title:	Mechanistic studies of new oximes reactivators of human butyryl cholinesterase inhibited by cyclosarin and sarin.
Authors:	de Lima WE, Francisco A, da Cunha EF, Radic Z, Taylor P, França TC, Ramalho TC
Link:	https://www.ncbi.nlm.nih.gov/pubmed/27125569?dopt=Abstract
DOI:	10.1080/07391102.2016.1178173
Publication:	Journal of biomolecular structure & dynamics
Keywords:	butyrylcholinesterase; docking; mechanistic studies and chemometrics; neurotoxic agents; oximes;
PMID:	27125569	Category:	J Biomol Struct Dyn	Date Added:	2019-06-20
Dept Affiliation:	CHEMISTRY 1 a Laboratory of Molecular Modeling, Chemistry Department , Federal University of Lavras , Lavras , MG 37200-000 , Brazil. 2 b Skaggs School of Pharmacy and Pharmaceutical Sciences , University of California at San Diego , San Diego , CA , USA. 3 c Laboratory of Molecular Modeling Applied to the Chemical and Biological Defense (LMCBD) , Military Institute of Engineering , Rio de Janeiro , RJ 22290-270 , Brazil. 4 d Department of Chemistry & Biochemistry , Concordia University , Montreal , QC , Canada. 5 e Faculty of Informatics and Management, Center for Basic and Applied Research , University of Hradec Kralove , Hradec Kralove , Czech Republic.

Description:

Mechanistic studies of new oximes reactivators of human butyryl cholinesterase inhibited by cyclosarin and sarin.

J Biomol Struct Dyn. 2017 May;35(6):1272-1282

Authors: de Lima WE, Francisco A, da Cunha EF, Radic Z, Taylor P, França TC, Ramalho TC

Abstract

Butyryl cholinesterase (BChE) has been seen as a key enzyme in the search for new strategies in the treatment of poisoning by organophosphates (OPs), since human BChE (HssBChE), complexed with the appropriate oxime, can be a suitable scavenger and deactivator for OPs in the blood stream. However, the efficacy of HssBChE is limited by its strict stoichiometric scavenging, slow reactivation, and propensity for aging. The improvement of the reactivation rate by new and more efficient oximes could contribute to mitigate this problem and increase the HssBChE efficiency as scavenger. Several oximes have been synthesized and tested with this goal, some with promising results, but the mechanistic aspects of the reactivation reaction are not fully understood yet. In order to better investigate this mechanism, docking and mixed quantum and molecular mechanics combined with principal components analysis were performed here to evaluate the capacity of reactivation and determine the preferred route for the reactivation reaction of two new oximes on HssBChE inhibited by the neurotoxic agents cyclosarin and sarin. Plots of potential energies were calculated and all the transition states of the reactional mechanism were determined. Our results showed a good correlation with experimental data and pointed to the most efficient oxime with both OPs. The protocol used could be a suitable tool for a preliminary evaluation of the HssBChE reactivation rates by new oximes.

PMID: 27125569 [PubMed - indexed for MEDLINE]

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