Miguel Constantino and his group were examined the cytotoxicity of old material which is Acrylic reline resins by using salivary acetylcholinesterase as substrate, therefore I would like to examine the cytotoxicity of a new material (polyamide) and I'm searching about enzyme substrate to do my work. Thank you
Dear Ali,
Since your compound is an amide, I suggest that you test its cytotoxicity using amidase enzymes.
The following papers might serve as a starting point for your experiments.
1- ACS Chem Biol. 2015 Aug 21;10(8):1838-46. doi: 10.1021/acschembio.5b00114. Epub 2015 Apr 15.
A Potent Systemically Active N-Acylethanolamine Acid Amidase Inhibitor that Suppresses Inflammation and Human Macrophage Activation.
Ribeiro A1, Pontis S1, Mengatto L1, Armirotti A1, Chiurchiù V2, Capurro V1, Fiasella A1, Nuzzi A1, Romeo E1, Moreno-Sanz G3, Maccarrone M3,4, Reggiani A1,Tarzia G5, Mor M6, Bertozzi F1, Bandiera T1, Piomelli D1,7.
Author information
Abstract
Fatty acid ethanolamides such as palmitoylethanolamide (PEA) and oleoylethanolamide (OEA) are lipid-derived mediators that potently inhibit pain and inflammation by ligating type-α peroxisome proliferator-activated receptors (PPAR-α). These bioactive substances are preferentially degraded by the cysteine hydrolase, N-acylethanolamine acid amidase (NAAA), which is highly expressed in macrophages. Here, we describe a new class of β-lactam derivatives that are potent, selective, and systemically active inhibitors of intracellular NAAA activity. The prototype of this class deactivates NAAA by covalently binding the enzyme's catalytic cysteine and exerts profound anti-inflammatory effects in both mouse models and human macrophages. This agent may be used to probe the functions of NAAA in health and disease and as a starting point to discover better anti-inflammatory drugs.
PMID:
25874594
2- ArticleBiotechnology Letters
March 1984, Volume 6, Issue 3, pp 149-154
A study of the inhibition of an amidase with a wide substrate spectrum and its consequences for the bioconversion of nitriles
M. Maestracci , K. Bui , A. Thiéry , A. Arnaud , P. Galzy
Summary
TheBrevibacterium sp. R 312 strain possesses a nitrile-hydratase and an amidase, both with a wide substrate spectrum. These two enzymes can be used for the bioconversion of nitriles into the corresponding organic acids: the actions of three types of compounds (nitriles, amides and acids) on the activity of the amidase are reported in the present work.
3- A Novel Mechanism Underlies the Hepatotoxicity of Pyrazinamide
Tung-Yuan Shiha,
Chien-Yi Paib,
Ping Yangb,
Wen-Liang Changb,
Ning-Chi Wangc and
Oliver Yoa-Pu Hua,b
+Author Affiliations
aGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan
bSchool of Pharmacy, National Defense Medical Center, Taipei, Taiwan
cDivision of Infectious Disease and Tropical Medicine, Tri-Service General Hospital, Taipei, Taiwan
Next Section
ABSTRACT
Relatively little is known about the hepatotoxicity of pyrazinamide (PZA). PZA requires activation by amidase to form pyrazinoic acid (PA). Xanthine oxidase then hydroxylates PA to form 5-hydroxypyrazinoic acid (5-OH-PA). PZA can also be directly oxidized to form 5-OH-PZA. Before this study, it was unclear which metabolic pathway or PZA metabolites led to hepatotoxicity. This study determines whether PZA metabolites are responsible for PZA-induced hepatotoxicity. PZA metabolites were identified and cytotoxicity in HepG2 cells was assessed. Potential PZA and PA hepatotoxicity was then tested in rats. Urine specimens were collected from 153 tuberculosis (TB) patients, and the results were evaluated to confirm whether a correlation existed between PZA metabolite concentrations and hepatotoxicity. This led to the hypothesis that coadministration of amidase inhibitor (bis-p-nitrophenyl phosphate [BNPP]) decreases or prevents PZA- and PZA metabolite-induced hepatotoxicity in rats. PA and 5-OH-PA are more toxic than PZA. Electron microscopy showed that PZA and PA treatment of rats significantly increases aspartate transaminase (AST) and alanine aminotransferase (ALT) activity and galactose single-point (GSP) levels (P < 0.005). PA and 5-OH-PA levels are also significantly correlated with hepatotoxicity in the urine of TB patients (P < 0.005). Amidase inhibitor, BNPP, decreases PZA-induced, but not PA-induced, hepatotoxicity. This is the first report of a cell line, animal, and clinical trial confirming that the metabolite 5-OH-PA is responsible for PZA-induced hepatotoxicity.
Hoping this will be helpful,
Rafik
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