scholarly journals The study of complexation of 5,17-bis-(n-tolyliminomethyl)- 25,27-dipropoxycalix[4]arene with benzoic acids by rp hplc and molecular modeling methods

2013 ◽  
Vol 11 (3(43)) ◽  
pp. 3-8
Author(s):  
O. I. Kalchenko ◽  
S. O. Cherenok ◽  
V. I. Kalchenko ◽  
A. V. Solovyov ◽  
V. V. Gorbatchuk
Keyword(s):  
Molecular Modeling ◽  
Benzoic Acids ◽  
Modeling Methods ◽  
Rp Hplc

scholarly journals Recognition and Binding of Aliphatic Dicarboxylic Acids C4 – C10 by Diiminocalix[4]arene

2019 ◽  
Vol 7 (2) ◽  
pp. 61-67
Author(s):  
Olga Kalchenko ◽  
Andrew Solovyov ◽  
Vitaly Kalchenko
Keyword(s):  
Molecular Modeling ◽  
Dicarboxylic Acids ◽  
Supramolecular Complexes ◽  
Cooh Group ◽  
Organic Solution ◽  
Modeling Methods ◽  
Rp Hplc ◽  
Aliphatic Dicarboxylic Acids ◽  
The Stability ◽  
Upper Rim

Host-Guest complexation of 5,17-bis-(N-tolyliminomethyl)-25,27-dipropoxycalix[4]arenewithaliphatic dicarboxylicacidsC4 – C10 hasbeenstudiedin water-organic solution by the RP HPLC and molecular modeling methods. The stability constants (log KA =2.56– 3.05) of the supramolecular complexes are depended on structure, pKa and log Pvalues of the acids. The complexation is determined by the hydrogen bonds of the COOH group of the dicarboxylic acids with nitrogen atoms at the upper rim or oxygen atoms at the lower rim of the calixarene.

Investigation of Isoindolo[2,1-a]quinoxaline-6-imines as Topoisomerase I Inhibitors with Molecular Modeling Methods

2017 ◽  
Vol 13 (3) ◽  
Author(s):  
Balazs Balogh ◽  
Anna Carbone ◽  
Virginia Spanò ◽  
Alessandra Montalbano ◽  
Paola Barraja ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Topoisomerase I ◽  
Modeling Methods ◽  
Topoisomerase I Inhibitors

Interaction of donepezil with tau protein: Insights from surface plasmon resonance and molecular modeling methods

2021 ◽  
pp. 115924
Author(s):  
Sepideh Najar-Ahmadi ◽  
Hossein Haghaei ◽  
Safar Farajnia ◽  
Reza Yekta ◽  
Jafar Ezzati Nazhad Dolatabadi ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Molecular Modeling ◽  
Surface Plasmon ◽  
Tau Protein ◽  
Plasmon Resonance ◽  
Modeling Methods

Studies on the interaction mechanism between CXS and papain by spectroscopic and molecular modeling methods

2012 ◽  
Vol 39 (3) ◽  
pp. 1257-1267 ◽  
Author(s):  
Xiaoli Xi ◽  
Manman Yang ◽  
Tinggui Cheng ◽  
Liwei Zhang ◽  
Pin Yang
Keyword(s):  
Molecular Modeling ◽  
Interaction Mechanism ◽  
Modeling Methods

scholarly journals Effect of Heldanamycin Binding on the Thr90 Phosphorylation Site of Hsp90

2021 ◽  
Vol 4 (3) ◽  
pp. e00145
Author(s):  
K.A. Shcherbakov ◽  
D.S. Shcherbinin ◽  
A.V. Veselovsky
Keyword(s):  
Prostate Cancer ◽  
Transcription Factor ◽  
Androgen Receptor ◽  
Molecular Modeling ◽  
Phosphorylation Site ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitor ◽  
Inhibitor Binding ◽  
Atp Binding Site ◽  
Modeling Methods

Prostate cancer is hormone-dependent and the androgen receptor (AR) is involved in its development. AR is a transcription factor that is activated by ligand binding, result in its translocation into the nucleus, where it initiates gene transcription. In an inactive state in cytoplasm AR exists as a complex with heat shock protein 90 (HSP90) and some other proteins. When the agonist binds, a conformational change in AR occurs, resulting in HSP90 and other chaperones dissociating. Recently it has been shown that for the dissociation of the HSP90-AR complex and the translocation of the latter into the nucleus, phosphorylation of the Thr-90 residue of the N-terminal domain of HSP90 is necessary. In this work, the effect of the HSP90 inhibitor, heldanamycin, interacting with the ATP-binding site, on the Thr90 phosphorylation site was investigated by molecular modeling methods. It has been shown that inhibitor binding slightly affects the size and mobility of cavity around Thr90. It is suggested that inhibitor binding to HSP90 does not result in changing the protein structure and does not influence on protein phosphorylation, and partially explains low effectiveness of such type of drugs in the therapy of prostate cancer.

scholarly journals The interaction of clenbuterol hydrochloride with bovine hemoglobin using spectroscopic techniques and molecular modeling methods

2009 ◽  
Vol 23 (5-6) ◽  
pp. 271-279 ◽  
Author(s):  
Yun Wu ◽  
Hui Mao ◽  
Bo Zhao ◽  
Jian Shen
Keyword(s):  
Molecular Modeling ◽  
Protein Secondary Structure ◽  
Binding Mode ◽  
Bovine Hemoglobin ◽  
Spectroscopic Techniques ◽  
Electronic Interaction ◽  
Physiological Conditions ◽  
Modeling Methods ◽  
Clenbuterol Hydrochloride ◽  
Hoff Equation

The interaction of clenbuterol hydrochloride (CL) to bovine hemoglobin (BHb) under physiological conditions was investigated by using UV-vis absorption, fluorescence, circular dichroism (CD) and molecular modeling. The fluorescence intensity of BHb decreased regularly with the gradual increasing concentration of CL. It is observed that there was a prominent interaction between CL and BHb. The fluorescence data revealed that the fluorescence quenching is a static process, and the thermodynamic parameters were calculated according to the Van't Hoff equation. The alternations of protein secondary structure in the presence of CL were determined by the evidence of CD. Molecular modeling study that corroborate our experimental results revealed that the binding mode of CL–BHb complex could be attributed to the hydrophobic interaction and hydrogen bonding, but electronic interaction cannot be excluded.

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