Enthalpy and enzyme activity of modified histidine residues of adenosine deaminase and diethyl pyrocarbonate complexes

Ataie, G.; Moosavi-Movahedi, Ali Akbar; Saboury, Ali Akbar; Hakimelahi, G. H.; Hwu, Jih Ru; Tsay, Shwu‐Chen

doi:10.1016/s0141-8130(99)00113-0

Cited by 18 publications

(5 citation statements)

References 21 publications

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“…PTMs of proteins through synthetic methods provide opportunities to precisely attach a wide range of moieties on demand to create new proteins. Site-specific conjugation empowers proteins with new characteristics, further expanding their applications, specifically in diagnosis and therapeutics (Ataie et al, 2000; Khajeh et al, 2001; Safarian et al, 2003; Hashemnia et al, 2006; Tavakoli et al, 2006). A better understanding of the protein structure–function relationship is another invaluable achievement of the synthetic modification of proteins.…”

Section: Enzymementioning

confidence: 99%

Protein click chemistry and its potential for medical applications

Amiri,

Abedanzadeh,

Davaeil

et al. 2024

Quart. Rev. Biophys.

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A revolution in chemical biology occurred with the introduction of click chemistry. Click chemistry plays an important role in protein chemistry modifications, providing specific, sensitive, rapid, and easy-to-handle methods. Under physiological conditions, click chemistry often overlaps with bioorthogonal chemistry, defined as reactions that occur rapidly and selectively without interfering with biological processes. Click chemistry is used for the posttranslational modification of proteins based on covalent bond formations. With the contribution of click reactions, selective modification of proteins would be developed, representing an alternative to other technologies in preparing new proteins or enzymes for studying specific protein functions in different biological processes. Click-modified proteins have potential in diverse applications such as imaging, labeling, sensing, drug design, and enzyme technology. Due to the promising role of proteins in disease diagnosis and therapy, this review aims to highlight the growing applications of click strategies in protein chemistry over the last two decades, with a special emphasis on medicinal applications.

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Section: Enzymementioning

confidence: 99%

Protein click chemistry and its potential for medical applications

Amiri,

Abedanzadeh,

Davaeil

et al. 2024

Quart. Rev. Biophys.

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“…The enthalpy, equilibrium and inhibition constants for binding were obtained. 17,18 On the other hand, performing QSAR analysis for several series of drugs, macromolecules enzyme and biological active compounds is now well appreciated. Kinetic parameters were used for the QSAR analysis and as such, we found some theoretical descriptors which correlated the binding affinity of ADA towards several adenine nucleosides as inhibitors.…”

Section: Introductionmentioning

confidence: 99%

Effects of Dimaine, Diacid and Dintitro Derivatives on the Inhibition of Adenosine Deaminase; Experimental, Molecular Docking and QSAR Studies

2009

Bulletin of the Korean Chemical Society

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Effects of some diacid, diamine and dinitro aromatic compounds on the structure and activity of adenosine deaminase (ADA) were investigated by UV-Vis spectrophotometry in 50 mM phosphate buffer at pH = 7.5 and 27 o C and molecular docking studies. The results showed that all tested ligands are showing inhibition; five ligands are uncompetitive and other two ligands are mixed of competitive and noncompetetive inhibitors with majority of competitive behavior. For the later case analysis was done based on competitive inhibition. Diacids have larger size and higher inhibition constant (KI) relative to others. A logical correlation between calculated free energy of binding and experimental values was obtained for un-competitive. Experimental and calculated data showed that competitive inhibitors are distributed near the active site of enzyme and form several cluster of ranks, whereas uncompetitive inhibitors bind to the enzyme-substrate complex and distributed far from the active site. Results of structure-activity relationship showed that, larger, more hydrophobe, less spherical and more aromatic ligands have higher inhibition constants.

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“…ITC gives invaluable information about biomacromolecule-ligand interactions. During the last two years we attempted to study the metal ion binding chemistry of different proteins [4][5][6][7][8][9][10][11][12]. They will change the conformational stability and form aggregates.…”

Section: Introductionmentioning

confidence: 99%

A New Approach for Titration Calorimetric Data Analysis on the Binding of Magnesium Ion with Myelin Basic Protein

2008

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The interaction of the myelin basic protein (MBP) from the bovine central nervous system with divalent magnesium ion was studied by isothermal titration calorimetry at 27°C in aqueous solution. A simple rapid method for determination of the dissociation binding constants for Mg 2+ -MBP interaction was introduced using the isothermal titration calometric data. The binding isotherm for Mg 2+ -MBP interaction is easily obtained by carrying out a titration calorimetric experiment using only one set of concentrations of MBP. There are two identical independent intrinsic association constants equal to 0.021 μmol·L −1 in the first-and second-binding sites, respectively.

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Enthalpy and enzyme activity of modified histidine residues of adenosine deaminase and diethyl pyrocarbonate complexes

Cited by 18 publications

References 21 publications

Protein click chemistry and its potential for medical applications

Protein click chemistry and its potential for medical applications

Effects of Dimaine, Diacid and Dintitro Derivatives on the Inhibition of Adenosine Deaminase; Experimental, Molecular Docking and QSAR Studies

A New Approach for Titration Calorimetric Data Analysis on the Binding of Magnesium Ion with Myelin Basic Protein

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