Thermodynamic determination of the binding constants of angiotensin‐converting enzyme inhibitors by a displacement method

Andújar‐Sánchez, Montserrat; Jara‐Pérez, Vicente; Cámara-Artigas, A.

doi:10.1016/j.febslet.2007.06.048

Cited by 16 publications

(7 citation statements)

References 34 publications

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“…The interaction between the ligand and receptor contains two types of binding: specific and non-specific. “Specific binding” represents the “lock–key” interaction with strong affinity, while “non-specific binding” refers to the binding of non-physiological origin with weak affinity. , The values of association constant K a between GF-6 and ACE were 4.67 × 10 5 , 1.63 × 10 4 , and 9.78 × 10 3 M –1 at 15, 20, and 25 °C, respectively, while those reported for captopril, enalaprilat, and lisinopril are 7.5 × 10 7 , 1.9 × 10 8 , and 6.2 × 10 8 M –1 , respectively . These studies showed that all three inhibitors bound with ACE at the active site via “specific binding”, while GF-6 interacted with ACE via “non-specific binding”.…”

Section: Resultsmentioning

confidence: 95%

Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from Saurida elongata

Lan

Sun

Muhammad

et al. 2018

J. Agric. Food Chem.

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Angiotensin-converting enzyme (ACE) inhibitory peptides derived from food protein exhibited antihypertensive effects by inhibiting ACE activity. In this work, the interaction between ACE inhibitory peptide GMKCAF (GF-6) and ACE was studied by isothermal titration calorimetry (ITC), molecular docking, ultraviolet absorption spectroscopy, fluorescence spectroscopy, and circular dichroism spectroscopy. Experimental results revealed that the binding of GF-6 to ACE was a spontaneous exothermic process driven by both enthalpy and entropy. The interaction occurred via a static quenching mechanism and involved the alteration of the conformation of ACE. In addition, ITC and molecular docking results indicated binding of GF-6 to ACE via multiple binding sites on the protein surface. This study could be deemed helpful for the better understanding of the inhibitory mechanism of ACE inhibitory peptides.

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Section: Resultsmentioning

confidence: 95%

Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from Saurida elongata

Lan

Sun

Muhammad

et al. 2018

J. Agric. Food Chem.

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“…Upon ligand binding, the changes in the solvent accessible area can be analyzed and related to the measured thermodynamic parameters. Empirical equations can be derived to relate the experimental thermodynamics with structure-based calculated parameters based on analysis of the enzyme's solvent-accessible surface area (Livingstone et al, 1991;Andú jar-Sánchez et al, 2007;Fernando et al, 2007). The thermodynamic parameters were calculated for unligated enzyme and compared with the substrate-bound enzyme using Vadar web server (Volume, Area, Dihedral Angle Reporter), which is a compilation of more than 15 different algorithms and programs for analyzing and assessing peptide and protein structures from their PDB coordinate data (Willard et al, 2003).…”

Section: Dissection Of Ligand-protein Interaction Energiesmentioning

confidence: 99%

Binding dynamics and energetic insight into the molecular forces driving nucleotide binding by guanylate kinase

Kandeel

Kitade

2010

J of Molecular Recognition

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Plasmodium deoxyguanylate pathways are an attractive area of investigation for future metabolic and drug discovery studies due to their unique substrate specificities. We investigated the energetic contribution to guanylate kinase substrate binding and the forces underlying ligand recognition. In the range from 20 to 35°C, the thermodynamic profiles displayed marked decrease in binding enthalpy, while the free energy of binding showed little changes. GMP produced a large binding heat capacity change of -356 cal mol(-1) K(-1), indicating considerable conformational changes upon ligand binding. Interestingly, the calculated ΔCp was -32 cal mol(-1) K(-1), indicating that the accessible surface area is not the central change in substrate binding, and that other entropic forces, including conformational changes, are more predominant. The thermodynamic signature for GMP is inconsistent with rigid-body association, while dGMP showed more or less rigid-body association. These binding profiles explain the poor catalytic efficiency and low affinity for dGMP compared with GMP. At low temperature, the ligands bind to the receptor site under the effect of hydrophobic forces. Interestingly, by increasing the temperature, the entropic forces gradually vanish and proceed to a nonfavorable contribution, and the interaction occurs mainly through bonding, electrostatic forces, and van der Waals interactions.

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“…In the work of Andújar-Sánchez et al [46], the binding constants of angiotensin-converting enzyme inhibitors were determined by a displacement method of ITC. Somatic angiotensin I-converting enzyme (s-ACE) plays a central role in blood pressure regulation and has been the target of most antihypertensive drugs.…”

Section: Rf-1 [X]mentioning

confidence: 99%

“…The relative potency of the inhibitors was determined to be enalaprilat>lisinopril>captopril. Andújar-Sánchez et al analyzed the thermodynamic behavior of the binding process using the new structural information provided by the ACE structures, as well as the conformational changes that occurred upon binding [46].…”

Section: Rf-1 [X]mentioning

confidence: 99%

Applications of isothermal titration calorimetry in protein science

Liang

2008

ABBS

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During the past decade, isothermal titration calorimetry (ITC) has developed from a specialist method for understanding molecular interactions and other biological processes within cells to a more robust, widely used method. Nowadays, ITC is used to investigate all types of protein interactions, including protein-protein interactions, protein-DNA/RNA interactions, protein-small molecule interactions and enzyme kinetics; it provides a direct route to the complete thermodynamic characterization of protein interactions. This review concentrates on the new applications of ITC in protein folding and misfolding, its traditional application in protein interactions, and an overview of what can be achieved in the field of protein science using this method and what developments are likely to occur in the near future. Also, this review discusses some new developments of ITC method in protein science, such as the reverse titration of ITC and the displacement method of ITC.

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Thermodynamic determination of the binding constants of angiotensin‐converting enzyme inhibitors by a displacement method

Cited by 16 publications

References 34 publications

Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from Saurida elongata

Studies on the Interaction between Angiotensin-Converting Enzyme (ACE) and ACE Inhibitory Peptide from Saurida elongata

Binding dynamics and energetic insight into the molecular forces driving nucleotide binding by guanylate kinase

Applications of isothermal titration calorimetry in protein science

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