Comparative study of the binding between chlorogenic acid and four proteins by isothermal titration calorimetry, spectroscopy and docking methods

Zhang, Miao; Zhang, Ning; Lu, Xinluan; Li, Wenjin; Wang, Ruiyong; Chang, Junbiao

doi:10.1007/s43440-022-00369-w

Cited by 4 publications

(4 citation statements)

References 45 publications

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“…It is observed that the binding constants ( K a ) and the number of binding sites ( n ) both decrease with the increase in temperature in Table 5. It further confirms that the interaction between theophylline and caffeine and HSA is static quenching 48,50 . The number of binding sites ( n ) is approximately equal to 1, indicating that Tph (or Caf) has just a single binding site in HSA.…”

Section: Resultssupporting

confidence: 66%

“…The value of K q is much larger than the maximum diffusion collision rate constant. It can be inferred that the binding of theophylline and caffeine with HSA is caused by static quenching 48 …”

Section: Resultsmentioning

confidence: 99%

“…It can be inferred that the binding of theophylline and caffeine with HSA is caused by static quenching. 48…”

Section: Molecular Modellingmentioning

confidence: 99%

“…It further confirms that the interaction between theophylline and caffeine and HSA is static quenching. 48,50 The number of binding sites (n) is approximately equal to 1, indicating that Tph (or Caf) has just a single binding site in HSA. K a was in the order of 10 4 -10 5 L mol À1 , 51 indicating that the binding sites of small molecules and HSA were high-affinity sites.…”

Section: Binding Constants and Binding Sitesmentioning

confidence: 99%

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Investigation of steric hindrance effect on the interactions between four alkaloids and HSA by isothermal titration calorimetry and molecular docking

Lv,

Li,

Zhang

et al. 2024

J of Molecular Recognition

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The binding of four alkaloids with human serum albumin (HSA) was investigated by isothermal titration calorimetry (ITC), spectroscopy and molecular docking techniques. The findings demonstrated that theophylline or caffeine can bind to HAS, respectively. The number of binding sites and binding constants are obtained. The binding mode is a static quenching process. The effects of steric hindrance, temperature, salt concentration and buffer solution on the binding indicated that theophylline and HSA have higher binding affinity than caffeine. The fluorescence and ITC results showed that the interaction between HSA and theophylline or caffeine is an entropy‐driven spontaneous exothermic process. The hydrophobic force was the primary driving factor. The experimental results were consistent with the molecular docking data. Based on the molecular structures of the four alkaloids, steric hindrance might be a major factor in the binding between HSA and these four alkaloids. This study elucidates the mechanism of interactions between four alkaloids and HSA.

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Section: Resultssupporting

confidence: 66%

Section: Resultsmentioning

confidence: 99%

“…It can be inferred that the binding of theophylline and caffeine with HSA is caused by static quenching. 48…”

Section: Molecular Modellingmentioning

confidence: 99%