ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINE AND OF SULPHANILAMIDE

1940 ◽  
Vol 18b (11) ◽  
pp. 345-350 ◽  
Author(s):  
H. B. Collier
Keyword(s):  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Enzyme Inhibition ◽  
Ascaris Lumbricoides ◽  
Inhibitory Activity ◽  
Spectroscopic Observation ◽  
Hydroxyl Group ◽  
Bactericidal Action ◽  
Derivatives Of

Mammalian catalase and cytochrome oxidase are strongly inhibited by the hydroxy derivatives of phenothiazine and by p-hydroxylaminobenzenesulphonamide. Phenothiazine, sulphanilamide, and sulphapyridine have little or no effect. Cytochrome-c is irreversibly reduced by the hydroxy-sulphanilamide, as indicated by spectroscopic observation. The inhibitory activity apparently depends on the presence of the hydroxyl group. The relation of these findings to the vermicidal and bactericidal action of the compounds is discussed.Phenothiazine and thionol have no effect on Ascaris lumbricoides in vitro.

scholarly journals Antiallergic Activity of 6-Deoxy-2-O-methyl-6-(N-hexadecanoyl)amino-l-ascorbic Acid

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4684
Author(s):  
Kaori Miura ◽  
Hiroaki Matsuno ◽  
Yuji Iwaoka ◽  
Hideyuki Ito ◽  
Akihiro Tai
Keyword(s):  
Ascorbic Acid ◽  
Inhibitory Activity ◽  
Specific Antigen ◽  
Allergic Diseases ◽  
Food Allergies ◽  
Hydroxyl Group ◽  
Type I ◽  
Antiallergic Activity ◽  
Derivatives Of

Allergy is an excessive immune response to a specific antigen. Type I allergies, such as hay fever and food allergies, have increased significantly in recent years and have become a worldwide problem. We previously reported that an ascorbic acid derivative having palmitoyl and glucosyl groups, 2-O-α-d-glucopyranosyl-6-O-hexadecanoyl-l-ascorbic acid (6-sPalm-AA-2G), showed inhibitory effects on degranulation in vitro and on the passive cutaneous anaphylaxis (PCA) reaction in mice. In this study, several palmitoyl derivatives of ascorbic acid were synthesized and a structure–activity relationship study was performed to discover more potent ascorbic acid derivatives with degranulation inhibitory activity. 6-Deoxy-2-O-methyl-6-(N-hexadecanoyl)amino-l-ascorbic acid (2-Me-6-N-Palm-AA), in which a methyl group was introduced into the hydroxyl group at the C-2 position of ascorbic acid and in which the hydroxyl group at the C-6 position was substituted with an N-palmitoyl group, exhibited much higher inhibitory activity for degranulation in vitro than did 6-sPalm-AA-2G. 2-Me-6-N-Palm-AA strongly inhibit the PCA reaction in mice at lower doses than those of 6-sPalm-AA-2G. These findings suggest that 2-Me-6-N-Palm-AA may be a promising therapeutic candidate for allergic diseases.

scholarly journals The Physical Adsorption of Gelatinized Starch with Tannic Acid Decreases the Inhibitory Activity of the Polyphenol against α-Amylase

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1233
Author(s):  
Yueyi Wang ◽  
Shuangshuang Li ◽  
Fangting Bai ◽  
Junwei Cao ◽  
Lijun Sun
Keyword(s):  
Enzyme Inhibition ◽  
Tannic Acid ◽  
Inhibitory Activity ◽  
Adsorption Property ◽  
Physical Adsorption ◽  
Enzyme Active Site ◽  
Opposite Trend ◽  
Gelatinized Starch ◽  
The Difference

The effects of mixing orders of tannic acid (TA), starch, and α-amylase on the enzyme inhibition of TA were studied, including mixing TA with α-amylase before starch addition (order 1), mixing TA with pre-gelatinized starch before α-amylase addition (order 2) and co-gelatinizing TA with starch before α-amylase addition (order 3). It was found that the enzyme inhibition was always highest for order 1 because TA could bind with the enzyme active site thoroughly before digestion occurred. Both order 2 and 3 reduced α-amylase inhibition through decreasing binding of TA with the enzyme, which resulted from the non-covalent physical adsorption of TA with gelatinized starch. Interestingly, at low TA concentration, α-amylase inhibition for order 2 was higher than order 3, while at high TA concentration, the inhibition was shown with the opposite trend, which arose from the difference in the adsorption property between the pre-gelatinized and co-gelatinized starch at the corresponding TA concentrations. Moreover, both the crystalline structures and apparent morphology of starch were not significantly altered by TA addition for order 2 and 3. Conclusively, although a polyphenol has an acceptable inhibitory activity in vitro, the actual effect may not reach the expected one when taking processing procedures into account.

Synthesis and Biological Evaluation of Acetylcholinesterase Inhibitor Macakurzin C and Its Derivatives

Synlett ◽  
2015 ◽  
Vol 26 (08) ◽  
pp. 1131-1134 ◽  
Author(s):  
Hyoungsu Kim ◽  
Seung-Hoon Baek ◽  
Hongjun Jang
Keyword(s):  
Inhibitory Activity ◽  
Acetylcholinesterase Inhibitor ◽  
Biological Evaluation ◽  
Hydroxyl Groups ◽  
Structural Requirements ◽  
Ache Inhibitory Activity ◽  
Synthesis And Biological Evaluation ◽  
Derivatives Of

The derivatives of macakurzin C containing a modified D ring and protected C(3)/C(5)-hydroxyl groups were synthesized and their in vitro AChE inhibitory activity and neurotoxicity were evaluated to identify the structural requirements for the activities. The results indicated that C(3)-benzyl-protected derivative has a more potent AChE inhibitory activity (IC50, 2.6 μM) and a less neurotoxicity (GI50, >100 μM) than synthetic macakurzin C (IC50, 9.1 μM; GI50, 16.6 μM).

Synthesis and In Vitro Biological Activity Evaluation of Novel Imidazo [2,1-B][1,3,4] Thiadiazole as Anti-Alzheimer Agents

2020 ◽  
Vol 17 (5) ◽  
pp. 610-617
Author(s):  
Sara Azimi ◽  
Omidreza Firuzi ◽  
Aida Iraji ◽  
Afsaneh Zonouzi ◽  
Mahsima Khoshneviszadeh ◽  
...  
Keyword(s):  
Biological Activity ◽  
Inhibitory Activity ◽  
Phenyl Ring ◽  
Activity Evaluation ◽  
Butyryl Cholinesterase ◽  
Thiadiazole Derivatives ◽  
Derivatives Of

Background: Considering that AD is multifactorial in nature, novel series of imidazo [2,1-b][1,3,4] thiadiazole derivatives were designed to address the basic factors responsible for the disease. <p> Methods: These compounds were investigated as inhibitors of beta-site APP cleaving enzyme 1, acetylcholinesterase and butyryl cholinesterase. <p> Results: The BACE1 inhibitory results indicated that nitro phenyl substituted derivatives of imidazo [2,1-b][1,3,4] thiadiazole scaffold (R2 = m-NO2) demonstrated superior BACE1 inhibitory activity compared to other substituted moieties. In the BuChE assay, compounds 4h and 4l carrying meta NO2 at R2 of phenyl ring turned out to be potent inhibitors. <p> Conclusion: In conclusion, these novel synthesized derivatives seem to be promising anti-Alzheimer agents.

SEMI-SYNTHESIS AND EVALUATION OF HESPERETIN DERIVATIVES AS ACETYLCHOLINESTERASE INHIBITORS7

2018 ◽  
Vol 8 (4) ◽  
pp. 7-12
Author(s):  
Huan Tran The ◽  
Dao Tran Thanh
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Key Words ◽  
Inhibitory Activity ◽  
Acetylcholinesterase Inhibitory Activity ◽  
Ic50 Value ◽  
Ellman’S Method ◽  
Further Development ◽  
Derivatives Of

Background: Inhibition of acetylcholinesterase are regarded as one of promising approach to treat Alzheimer’s disease. Hesperetin is a potential flavonoid for further development in this direction. Objectives: Semi-synthesized and assayed for hesperetin derivatives’s acetylcholinesterase inhibitory activity in vitro. Materials and methods: Ester and ether derivatives of hesperetin were semi-synthesized. The semi-synthesis compounds were tested for acetylcholinesterase inhibitory activity in vitro according to the Ellman’s method. Results: Hesperetin is obtained by hydrolysing hesperidin. Then, two ester and two ether derivatives were semi-synthesized from hesperetin. The results showed that some of the semi-synthesis hesperetin derivatives displayed stronger acetylcholinesterase inhibitory activity than hesperetin. Among them, derivative 1 has the best activity with an IC50 value of 43.50 μM. Conclusions: Four hesperetin derivatives were semi-synthesized and investigated their acetylcholinesterase inhibitory activity, some of which showed improvement in activity. Key words: Hesperetin, semi-synthesis, inhibit, enzyme, acetylcholinesterase

THE RESPIRATION OF ASCARIS LUMBRICOIDES EGGS

1955 ◽  
Vol 33 (6) ◽  
pp. 1033-1046 ◽  
Author(s):  
Richard F. Passey ◽  
Donald Fairbairn
Keyword(s):  
Carbon Monoxide ◽  
Oxygen Consumption ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Ascaris Lumbricoides ◽  
Enzyme System ◽  
High Sensitivity ◽  
Partial Pressures ◽  
Rate Of Oxygen Consumption ◽  
Low Sensitivity

The rate of oxygen consumption of developing ascaris eggs decreased rapidly to a minimum after 1.5 days, and thereafter increased to a maximum at 10 days, when the embryos were vermiform. During the 10–20 day period, when the embryo matures and molts once in the egg, the respiration decreased steadily, and continued to decrease more slowly until at 140 days the rate was scarcely measurable. Nevertheless, the eggs remained viable and hatched readily in the mouse gut. Cytochrome c and cytochrome oxidase could not be detected by direct assay or isolation. However, the high sensitivity of the respiration to carbon monoxide (in the dark), to cyanide, and to azide, and the low sensitivity to carbon monoxide (in the light) and to decreasing partial pressures of oxygen, indicated that oxidases such as the flavoproteins, phenolases, and peroxidases were unlikely respiratory catalysts, and that cytochrome oxidase, or a similar and hitherto undescribed enzyme, was the major component of the terminal respiratory enzyme system.

scholarly journals The Physical Adsorption of Gelatinized Starch With Tannic Acid Decreases the Inhibitory Activity of the Polyphenol Against α-Amylase

2021 ◽  
Author(s):  
Yueyi Wang ◽  
Fangting Bai ◽  
Junwei Cao ◽  
Lijun Sun
Keyword(s):  
Enzyme Inhibition ◽  
Tannic Acid ◽  
Inhibitory Activity ◽  
Adsorption Property ◽  
Physical Adsorption ◽  
Alpha Amylase ◽  
Enzyme Active Site ◽  
Gelatinized Starch ◽  
The Difference

The effects of mixing orders of tannic acid (TA), starch and &alpha;-amylase on the enzyme inhibition of TA were studied, including mixing TA with &alpha;-amylase before starch addition (order 1), mixing TA with pre-gelatinized starch before &alpha;-amylase addition (order 2) and co-gelatinizing TA with starch before &alpha;-amylase addition (order 3). It was found that the enzyme inhibition was always highest for order 1 because TA could bind with the enzyme active site thoroughly before digestion occurred. Both order 2 and 3 reduced &alpha;-amylase inhibition through decreasing binding of TA with the enzyme, which resulted from the non-covalent physical adsorption of TA with gelatinized starch. Interestingly, at low TA concentration, &alpha;-amylase inhibition for order 2 was higher than order 3, while at high TA concentration, the inhibition was shown with opposite trend, which arose from the difference in the adsorption property between the pre-gelatinized and co-gelatinized starch at the corresponding TA concentrations. Besides, both the crystalline structures and apparent morphology of starch were not significantly altered by TA addition for order 2 and 3. Conclusively, although a polyphenol may have an acceptable inhibitory activity in vitro, the actual effect may not reach the expected one when taking processing procedures into account.

scholarly journals Design and synthesis of novel pyrazole-benzofuran hybrids: in vitro α-glucosidase inhibitory activity, kinetic and molecular modeling study

2021 ◽  
Author(s):  
Fateme Azimi ◽  
Homa Azizian ◽  
Mohammad Najafi ◽  
Ghadamali khodarahmi ◽  
Motahareh hassanzadeh ◽  
...  
Keyword(s):  
Active Site ◽  
Inhibitory Activity ◽  
Inhibitory Effect ◽  
Back Side ◽  
Binding Interaction ◽  
Dynamic Simulations ◽  
Standard Drug ◽  
Design And Synthesis ◽  
Derivatives Of

Abstract In this work, new derivatives of biphenyl pyrazole-benzofuran hybrids designed, synthesized and evaluated in vitro through enzymatic assay for inhibitory effect against α-glucosidase activity. Newly identified inhibitors were found to be four to eighteen folds more active with IC50 values in the range of 40.6 ± 0.2–164.3 ± 1.8 µM, as compared to the standard drug acarbose (IC50 = 750.0 ± 10.0 µM). Limited Structure-activity relationship was established. A kinetic binding study indicated that most active compound 8e acted as the competitive inhibitors of α-glucosidase with Ki = 38 µM. Molecular docking has also been performed to find the interaction modes responsible for the desired inhibitory activity. As expected, all pharmacophoric features used in the design of the hybrid, are involved in the interaction with the active site of the enzyme. In addition, molecular dynamic simulations showed compound 8e oriented vertically into the active site from mouth to the bottom and stabilized the enzyme domains by interacting with the interface of domain A and domain B and the back side of the active site while acarbose formed non-binding interaction with the residue belong to the domain A of the enzyme.

scholarly journals Study of the Anti-Proliferative Activity of 5-Substituted 4,7-Dimethoxy-1,3-Benzodioxole Derivatives of SY-1 fromAntrodia camphorataon Human COLO 205 Colon Cancer Cells

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Hsiu-Man Lien ◽  
Po-Tsun Kuo ◽  
Chao-Lu Huang ◽  
Jung-Yie Kao ◽  
Ho Lin ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Carcinoma Cells ◽  
Flow Cytometry Analysis ◽  
Antrodia Camphorata ◽  
Cycle Arrest ◽  
Normal Human ◽  
G1 Cell Cycle Arrest ◽  
Derivatives Of ◽  
Potent Inhibitory Activity

A set of 10 4,7-dimethoxy-1,3-benzodioxole derivatives based on a lead compound previously discovered by our group, SY-1, which was isolated fromAntrodia camphorata, were evaluated for theirin vitroinhibitory activity on human colorectal carcinoma cells (COLO 205). Structure-activity relationship studies of the 10 compounds indicated the importance of the chain length of the alkyl group at the 5-position, and the 2-propenyl substituent named “apiole” exhibited the most potent inhibitory activity. In the present study, we demonstrate that the SY-1 analogue “apiole” decreased the proliferation of COLO 205 cells, but not that of normal human colonic epithelial cells (FHC). The G0/G1 cell cycle arrest induced by apiole (75–225 μM) was associated with significantly increased levels of p53, p21 and p27 and decreased levels of cyclin D1. Concerning COLO 205 cell apoptosis, apiole (>150 μM) treatment significantly increased the levels of cleaved caspases 3, 8, 9 and bax/bcl-2 ratio and induced ladder formation in DNA fragmentation assay and sub-G1 peak in flow cytometry analysis. These findings suggest that apiole can suppress COLO 205 cell growth; however, the detailed mechanisms of these processes require further investigation.

scholarly journals Covalent binding of arylazido derivatives of cytochrome c to cytochrome oxidase

FEBS Letters ◽  
1977 ◽  
Vol 81 (1) ◽  
pp. 147-150 ◽  
Author(s):  
R. Bisson ◽  
Heidi Gutweniger ◽  
C. Montecucco ◽  
R. Colonna ◽  
A. Zanotti ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Covalent Binding ◽  
Derivatives Of
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