scholarly journals Potential of Bioactive Compounds of Arenga Vinegar as Traditional Medicine Through Reverse Docking Techniques

BIOEDUSCIENCE ◽  
2021 ◽  
Vol 5 (2) ◽  
Author(s):  
Diana Hernawati ◽  
Reza Fauzi Dwisandi ◽  
Egi Nuryadin
Keyword(s):  
Amino Acids ◽  
Acetic Acid ◽  
Traditional Medicine ◽  
Binding Site ◽  
Indigenous People ◽  
Binding Affinity ◽  
Bioactive Compounds ◽  
Hydrophobic Interactions ◽  
Level Control ◽  
Diabetes Drug

Background: Arenga vinegar (Arenga pinnata) has been trusted by the indigenous people of Kampung Kuta as traditional medicine, one of which is used as a diabetes medicine. For this reason, the aim of this study is to examine the bioactive compounds contained in arenga vinegar, namely acetic acid, which is predicted to be scientifically proven using reverse docking techniques. Methods: This research is descriptive qualitative research, by interpreting the data obtained from databases and software. Results: There is a binding pose between acetic acid and the sucrase-isomaltase enzyme, the lowest binding affinity value is -3.2 kcal/mol, and the binding site occurs hydrophobic interactions with the amino acids Trp327 (A), Asp355 (A), Ile392 (A), Trp470 (A), Phe604 (A), His629 (A), Trp586 (A) as well as hydrogen bonding to the amino acid Asp(472)A. Conclusions: The acetic acid-binding pose binds well to the sucrase-isomaltase enzyme so that the binding affinity value appears even though the value is not too low and the binding site occurs, this can be used as proof of the belief of the indigenous people of Kampung Kuta, namely the treatment of arenga vinegar as a diabetes drug, especially as a level control blood sugar.

A specific domain in alpha-catenin mediates binding to beta-catenin or plakoglobin

1997 ◽  
Vol 110 (15) ◽  
pp. 1759-1765 ◽  
Author(s):  
O. Huber ◽  
M. Krohn ◽  
R. Kemler
Keyword(s):  
Amino Acids ◽  
Binding Site ◽  
Mutational Analysis ◽  
Hydrophobic Interactions ◽  
Strong Support ◽  
Interaction Mechanism ◽  
Beta Catenin ◽  
Specific Domain ◽  
E Cadherin

The E-cadherin-catenin adhesion complex has been the subject of many structural and functional studies because of its importance in development, normal tissue function and carcinogenesis. It is well established that the cytoplasmic domain of E-cadherin binds either beta-catenin or plakoglobin, which both can assemble alpha-catenin into the complex. Recently we have identified an alpha-catenin binding site in beta-catenin and plakoglobin and postulated, based on sequence analysis, that these protein-protein interactions are mediated by a hydrophobic interaction mechanism. Here we have now identified the reciprocal complementary binding site in alpha-catenin which mediates its interaction with beta-catenin and plakoglobin. Using in vitro association assays with C-terminal truncations of alpha-catenin expressed as recombinant fusion proteins, we found that the N-terminal 146 amino acids are required for this interaction. We then identified a peptide of 27 amino acids within this sequence (amino acid positions 117–143) which is necessary and sufficient to bind beta-catenin or plakoglobin. As shown by mutational analysis, hydrophobic amino acids within this binding site are important for the interaction. The results described here, together with our previous work, give strong support for the idea that these proteins associate by hydrophobic interactions of two alpha-helices.

scholarly journals Binding affinity and stereoselectivity of local anesthetics in single batrachotoxin-activated Na+ channels.

1990 ◽  
Vol 96 (5) ◽  
pp. 1105-1127 ◽  
Author(s):  
G K Wang
Keyword(s):  
Binding Site ◽  
Binding Affinity ◽  
Local Anesthetics ◽  
Dwell Time ◽  
Hydrophobic Interactions ◽  
Na Channels ◽  
Structural Determinants ◽  
Planar Bilayers ◽  
Binding Domains ◽  
Hydrophobic Binding

Several local anesthetics (LA) have been previously shown to block muscle batrachotoxin (BTX)-activated Na+ channels in planar bilayers. The mean dwell time of different LA drugs, however, varies widely, from less than 10 ms to longer than several seconds. In this study, we have examined the structural determinants that govern the dwell time, the binding affinity, and the stereoselectivity of LA drugs using cocaine and bupivacaine homologues, RAC compounds, and their available stereoisomers. Our results from the structure-activity experiments reveal that (a) there are two apparent hydrophobic binding domains present in the LA binding site; one interacts with the aromatic moiety of the LA drugs, and the other interacts with the alkyl group attached to the tertiary amine of the LA drugs; (b) the LA mean dwell time and the binding affinity are largely determined by the hydrophobic interactions; (c) the LA binding site is highly stereoselective, with a difference in KD values over 50- and 6-fold for (+/-) cocaine and (+/-) bupivacaine, respectively; (d) the cocaine stereoselectivity is comparable among muscle, brain, and heart BTX-activated Na+ channels; and finally and most unexpectedly, (e) the stereoselectivity of LA drugs in BTX-activated Na+ channels appears greatly different from that reported in normal Na+ channels. Possible explanations for this difference are discussed.

Enhancement of Plasminogen Binding to U937 Cells and Fibrin by Complestatin

1997 ◽  
Vol 77 (01) ◽  
pp. 137-142 ◽  
Author(s):  
Kiyoshi Tachikawa ◽  
Keiji Hasurni ◽  
Akira Endo
Keyword(s):  
Binding Site ◽  
Binding Affinity ◽  
Blood Cells ◽  
Aminocaproic Acid ◽  
U937 Cells ◽  
Biochemical Basis ◽  
Equilibrium Binding ◽  
Pharmacological Stimulation ◽  
Endogenous Fibrinolysis ◽  
Stimulation Of

SummaryPlasminogen binds to endothelial and blood cells as well as to fibrin, where the zymogen is efficiently activated and protected from inhibition by α2-antiplasmin. In the present study we have found that complestatin, a peptide-like metabolite of a streptomyces, enhances binding of plasminogen to cells and fibrin. Complestatin, at concentrations ranging from 1 to 5 μM, doubled 125I-plasminogen binding to U937 cells both in the absence and presence of lipoprotein(a), a putative physiological competitor of plasminogen. The binding of 125I-plasminogen in the presence of complestatin was abolished by e-aminocaproic acid, suggesting that the lysine binding site(s) of the plasminogen molecule are involved in the binding. Equilibrium binding analyses indicated that complestatin increased the maximum binding of 125I-plasminogen to U937 cells without affecting the binding affinity. Complestatin was also effective in increasing 125I-plasminogen binding to fibrin, causing 2-fold elevation of the binding at ~1 μM. Along with the potentiation of plasminogen binding, complestatin enhanced plasmin formation, and thereby increased fibrinolysis. These results would provide a biochemical basis for a pharmacological stimulation of endogenous fibrinolysis through a promotion of plasminogen binding to cells and fibrin.

Racemization rates of 3,4-didehydro-2-amino acids

1989 ◽  
Vol 54 (12) ◽  
pp. 3381-3386 ◽  
Author(s):  
Libor Havlíček ◽  
Jan Hanuš ◽  
Jan Němeček
Keyword(s):  
Amino Acids ◽  
Acetic Acid ◽  
Acidic Medium

The racemization rates of amino acids in acidic medium (acetic acid) were studied. The sensitivity to racemization decreases in the order (E)-3,4-didehydroornithine > (E)-Nδ-Z-3,4-didehydroornithine >> (Z)-3,4-didehydronorvaline > ornithine, norvaline. (E)-3,4-Didehydroornithine is also relatively rapidly racemized on heating with 5 M or 0.05 M-HCl (100 °C).

scholarly journals Mitigating the Adverse Effects of Polychlorinated Biphenyl Derivatives on Estrogenic Activity via Molecular Modification Techniques

2021 ◽  
Vol 18 (9) ◽  
pp. 4999
Author(s):  
Wei He ◽  
Wenhui Zhang ◽  
Zhenhua Chu ◽  
Yu Li
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Hydrophobic Interaction ◽  
Oestrogen Receptor ◽  
Polychlorinated Biphenyl ◽  
Hydrophobic Interactions ◽  
Estrogenic Activity ◽  
Average Distance ◽  
Amino Acid Residues ◽  
Hydrophobic Amino Acid

The aim of this paper is to explore the mechanism of the change in oestrogenic activity of PCBs molecules before and after modification by designing new PCBs derivatives in combination with molecular docking techniques through the constructed model of oestrogenic activity of PCBs molecules. We found that the weakened hydrophobic interaction between the hydrophobic amino acid residues and hydrophobic substituents at the binding site of PCB derivatives and human oestrogen receptor alpha (hERα) was the main reason for the weakened binding force and reduced anti-oestrogenic activity. It was consistent with the information that the hydrophobic field displayed by the 3D contour maps in the constructed oestrogen activity CoMSIA model was one of the main influencing force fields. The hydrophobic interaction between PCB derivatives and oestrogen-active receptors was negatively correlated with the average distance between hydrophobic substituents and hydrophobic amino acid residues at the hERα-binding site, and positively correlated with the number of hydrophobic amino acid residues. In other words, the smaller the average distance between the hydrophobic amino acid residues at the binding sites between the two and the more the number of them, and the stronger the oestrogen activity expression degree of PCBS derivative molecules. Therefore, hydrophobic interactions between PCB derivatives and the oestrogen receptor can be reduced by altering the microenvironmental conditions in humans. This reduces the ability of PCB derivatives to bind to the oestrogen receptor and can effectively modulate the risk of residual PCB derivatives to produce oestrogenic activity in humans.

scholarly journals QUANTITATIVE ANALYSIS OF BIOACTIVE COMPOUNDS OF ARTEMISIA NILAGIRICA (CLARKE) PAMP. LEAF EXTRACT

2016 ◽  
pp. 183
Author(s):  
Parameswari P ◽  
Devika Rengaswamy
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Quantitative Analysis ◽  
Secondary Metabolites ◽  
Bioactive Compounds ◽  
Leaf Extract ◽  
Metabolic Reaction ◽  
Quantitative Investigation ◽  
Artemisia Nilagirica ◽  
Quantitative Examination

<p>ABSTRACT<br />Objective: The points of this exploration work were to decide the quantitative examination of bioactive mixes. Customarily, cutting edge meds rely<br />on the phytochemicals got from the plant source in bigger extents. Numerous bioactive auxiliary metabolites have a positive metabolic reaction on<br />different human diseases.<br />Methods: In the present examination, Artemisia nilagirica, leaves were gathered, dried, powdered and put away in hermetically sealed compartments<br />for quantitative investigation of phytochemicals according to standard strategies.<br />Results: The methanolic leaf concentrate of enrolled 4.33 mg of alkaloids, 1.22 mg of saponins, 12.4 mg of tannins, 24.3 mg of glycosides, 10.2 mg<br />terpenoids, 1.33 mg of coumarin, 59.4 mg of amino acids, 12.2 mg of fatty acids, 17.2 mg of flavonoids, 10.2 mg of phenols, and steroids in follows<br />separately.<br />Conclusion: The plant has a high helpful quality as far as an assortment of phytochemicals from leaf remove and had let to a sure level toward<br />extraction and refinement of specific bioactive mixes for human nourishment.<br />Keywords: Artemisia nilagirica, Secondary metabolites, Quantitative analysis, Leaf extract, Flavonoids.</p>

Synthesis and biological study of a flavone acetic acid analogue containing an azido reporting group designed as a multifunctional binding site probe

2005 ◽  
Vol 13 (8) ◽  
pp. 2717-2722 ◽  
Author(s):  
Krishnan Malolanarasimhan ◽  
Christopher C. Lai ◽  
James A. Kelley ◽  
Lynn Iaccarino ◽  
Della Reynolds ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Binding Site ◽  
Biological Study ◽  
Flavone Acetic Acid ◽  
Acid Analogue

scholarly journals Antiprotozoal Activity against Entamoeba histolytica of Plants Used in Northeast Mexican Traditional Medicine. Bioactive Compounds from Lippia graveolens and Ruta chalepensis

Molecules ◽  
2014 ◽  
Vol 19 (12) ◽  
pp. 21044-21065 ◽  
Author(s):  
Ramiro Quintanilla-Licea ◽  
Benito Mata-Cárdenas ◽  
Javier Vargas-Villarreal ◽  
Aldo Bazaldúa-Rodríguez ◽  
Isvar Kavimngeles-Hernández ◽  
...  
Keyword(s):  
Traditional Medicine ◽  
Entamoeba Histolytica ◽  
Bioactive Compounds ◽  
Antiprotozoal Activity ◽  
Ruta Chalepensis

Canonical interrelationships in morphological characters, yield and nutritional components of corn

2021 ◽  
Vol 8 ◽  
pp. 1-17
Author(s):  
Ivan Carvalho ◽  
José Antonio Gonzalez da Silva ◽  
Murilo Vieira Loro ◽  
Marlon Vinícius Rosa Sarturi ◽  
Danieli Jacoboski Hutra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bioactive Compounds ◽  
Yield Components ◽  
Zinc Content ◽  
Essential Amino Acids ◽  
Morphological Characters ◽  
Soluble Solids ◽  
World Population ◽  
Canonical Correlations ◽  
High Yields

The increase in the world population, the need to increase food production, both in quantity and quality, becomes increasingly prominent. The objective of this work was to identify the canonical correlations between yield components, morphological characters, micronutrients, bioactive compounds and amino acids in corn. The experimental design used was a randomized block containing 11 treatments arranged in three replications. The treatments consisted of 11 Top Crosses hybrid genotypes, these being made through crosses directed between a narrow genetic base tester hybrid for specific combining ability with 11 S5 inbred lines. It is inferred that groups considered yield components, secondary traits, bioactive compounds, micronutrients and amino acids are dependent. Promising characters are identified for the corn breeding for high yields, nutritional and energetic quality of corn grains. The indirect selection of grains with additions in essential amino acids can be directed to plants with superiority in height, mass and width of grains, phenols, flavonoids, soluble solids and zinc content.

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