Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Xiang, Yuhong; Duan, Lili; Ma, Qiang; Lv, Zizheng; Zhu, Ruizhi; Zhang, Zhuoyong

doi:10.1002/bio.3135

Cited by 18 publications

(13 citation statements)

References 49 publications

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“…The STD AMP factors showed that the molecular structure of each ligand affects the epitope mapping of each proton. Their preference for Sudlow site I as it was derived from the competitive STD NMR experiments confirms the existing literature data 46,49,59 .…”

Section: Discussionsupporting

confidence: 87%

“…The best fitting model was the one binding site model supporting the STD NMR competitive results. Finally, a K a ¼ 1.17 Â 10 5 M À1 is reported for the BSA-salvianic interaction 49 again estimated with fluorescence spectroscopy. In our experiments the binding was too low to estimate the K a or the thermodynamic parameters using ITC.…”

Section: Discussionmentioning

confidence: 75%

“…Rosmarinic and caffeic acid have been previously studied on their interaction with serum albumin (BSA or HSA) 9,[46][47][48] while there is only one study for the interaction of salvianic acid with BSA 49 . Fluorescence spectroscopy is the dominant technique used to elucidate these interactions.…”

Section: Discussionmentioning

confidence: 99%

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Unveiling the interaction profile of rosmarinic acid and its bioactive substructures with serum albumin

Papaemmanouil

Chatziathanasiadou

Chatzigiannis

et al. 2020

Journal of Enzyme Inhibition and Medicinal Chemistry

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Rosmarinic acid, a phytochemical compound, bears diverse pharmaceutical profile. It is composed by two building blocks: caffeic acid and a salvianic acid unit. The interaction profile, responsible for the delivery of rosmarinic acid and its two substructure components by serum albumin remains unexplored. To unveil this, we established a novel low-cost and efficient method to produce salvianic acid from the parent compound. To probe the interaction profile of rosmarinic acid and its two substructure constituents with the different serum albumin binding sites we utilised fluorescence spectroscopy and competitive saturation transfer difference NMR experiments. These studies were complemented with transfer NOESY NMR experiments. The thermodynamics of the binding profile of rosmarinic acid and its substructures were addressed using isothermal titration calorimetry. In silico docking studies, driven by the experimental data, have been used to deliver further atomic details on the binding mode of rosmarinic acid and its structural components.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 75%

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Unveiling the interaction profile of rosmarinic acid and its bioactive substructures with serum albumin

Papaemmanouil

Chatziathanasiadou

Chatzigiannis

et al. 2020

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Both free BSA and the AS-BSA complex demonstrated similar radii approximately 2.7 nm (Figure 2A and B), indicating that the compactness of BSA remained unchanged in the presence of AS. However, the fact that the RMSD value of the complex (Figure 2B) was slightly larger than that of the free BSA (Figure 2A) suggested that a synergic conformational change45 between AS and BSA might have occurred.…”

Section: Resultsmentioning

confidence: 98%

Fenretinide inhibits macrophage inflammatory mediators and controls hypertension in spontaneously hypertensive rats via the peroxisome proliferator-activated receptor gamma pathway

Lin¹,

Lee²,

Zhang³

et al. 2016

DDDT

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Fenretinide is a novel anticancer agent reported to exhibit anti-invasive and antimetastatic activities. It has also been shown to improve obesity and diabetes, although the effects of fenretinide on hypertension are still unknown, and the detailed mechanisms remain unclear. In this study, we have shown that treatment with lipopolysaccharide (LPS) decreased the expression of peroxisome proliferator-activated receptor γ (PPARγ) in RAW264.7 macrophages, and pretreatment with fenretinide reversed the effect of LPS on PPARγ expression. In addition, LPS-induced pro-inflammatory cytokine production, including tumor necrosis factor-α, interleukin 6, and monocyte chemoattractant protein 1 were dose-dependently reversed by fenretinide, and the effects of fenretinide on LPS-induced pro-inflammatory cytokine production were blocked by treatment with PPARγ antagonist. Moreover, fenretinide decreased LPS-induced inducible nitric oxide synthase expression and nitrogen oxide production. These effects were blocked by the pretreatment with PPARγ antagonist in a dose-dependent manner, indicating fenretinide activated PPARγ to exert anti-inflammation activity. In view of the role of inflammation in hypertension and the anti-inflammatory action of fenretinide, we found that administration of fenretinide in spontaneously hypertensive rats significantly decreased blood pressure. Taken together, these results indicate that fenretinide might be a potent antihypertensive agent that works by suppressing inflammation via activating PPARγ.

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“…44 Both free BSA and the AS-BSA complex demonstrated similar radii approximately 2.7 nm ( Figure 2A and B ), indicating that the compactness of BSA remained unchanged in the presence of AS. However, the fact that the RMSD value of the complex ( Figure 2B ) was slightly larger than that of the free BSA ( Figure 2A ) suggested that a synergic conformational change 45 between AS and BSA might have occurred.…”

Section: Resultsmentioning

confidence: 98%

Combined computational and experimental studies of molecular interactions of albuterol sulfate with bovine serum albumin for pulmonary drug nanoparticles

Lin

Cui

Wang

et al. 2016

DDDT

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Albumin-based nanoparticles (NPs) are a promising technology for developing drug-carrier systems, with improved deposition and retention profiles in lungs. Improved understanding of these drug–carrier interactions could lead to better drug-delivery systems. The present study combines computational and experimental methods to gain insights into the mechanism of binding of albuterol sulfate (AS) to bovine serum albumin (BSA) on the molecular level. Molecular dynamics simulation and surface plasmon resonance spectroscopy were used to determine that there are two binding sites on BSA for AS: the first of which is a high-affinity site corresponding to AS1 and the second of which appears to represent the integrated functions of several low-affinity sites corresponding to AS2, AS3, and AS8. AS1 was the strongest binding site, established via electrostatic interaction with Glu243 and Asp255 residues in a hydrophobic pocket. Hydrogen bonds and salt bridges played a main role in the critical binding of AS1 to BSA, and water bridges served a supporting role. Based upon the interaction mechanism, BSA NPs loaded with AS were prepared, and their drug-loading efficiency, morphology, and -release profiles were evaluated. Successful clinical development of AS-BSA-NPs may improve therapy and prevention of bronchospasm in patients with reversible obstructive airway disease, and thus provide a solid basis for expanding the role of NPs in the design of new drug-delivery systems.

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Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Cited by 18 publications

References 49 publications

Unveiling the interaction profile of rosmarinic acid and its bioactive substructures with serum albumin

Unveiling the interaction profile of rosmarinic acid and its bioactive substructures with serum albumin

Fenretinide inhibits macrophage inflammatory mediators and controls hypertension in spontaneously hypertensive rats via the peroxisome proliferator-activated receptor gamma pathway

Combined computational and experimental studies of molecular interactions of albuterol sulfate with bovine serum albumin for pulmonary drug nanoparticles

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