In vitro study on the interaction of methoxyflurane with human serum albumin: Phenotypic characterization

Xing, Aning; Jia, Bin; Li, Xuan; Zhang, Zhaodi; Gu, Guangying; Wang, Guonian

doi:10.1016/j.jfluchem.2013.05.006

Cited by 8 publications

(6 citation statements)

References 34 publications

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“…The results were listed in Table 2. The decreasing trend of binding constants (K a ) with increasing temperature was in accordance with K sv 's dependence on temperature, as mentioned above [16] . As shown in Table 2, the K a between Cefpirome and Trypsin decreased with increasing temperature, further suggesting that the quenching was a static process.…”

Section: Fluorescence Quenching Of Trypsin By Cefpiromesupporting

confidence: 85%

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

Liu¹,

Wang²,

Bian³

et al. 2017

JABST

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The interaction between Cefpirome and Trypsin was studied using multi-spectroscopy and molecular docking methods. The results showed that quenching mechanism of the Trypsin-Cefpirome system was probably static. The main interaction force was electrostatic force, and the number of binding sites in this system was approximately equal to 1. The quenching curves indicated that the tyrosine and tryptophan residues were both involved in the reaction. Synchronous fluorescence spectroscopy further confirmed that the main binding site was closer to tryptophan residues. The distance (r) between Trypsin and Cefpirome was less than 7 nm, which indicated that the energy transfer from Trypsin to Cefpirome was non-radiative energy transfer. The values of the Hill's coefficients showed that there was negative cooperativity in the interaction between Cefpirome and Trypsin.

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Section: Fluorescence Quenching Of Trypsin By Cefpiromesupporting

confidence: 85%

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

Liu¹,

Wang²,

Bian³

et al. 2017

JABST

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“…where: F 0 -fluorescence in the absence of quenching molecules, F − fluorescence in the presence of quencher, [Q] − quenchers concentration, K b − binding constant, n − number of binding sites Our constants were: K b ≈ 0.015 × 10 3 M −1 and n = 0.3. When calculated "n" is very close to 1, indicating only one high affinity binding site [29]. Received quite low value of "n" (Fig.…”

Section: Resultsmentioning

confidence: 84%

“…This significant difference in binding constants results probably is related to protein structure and function. Alpha-synuclein has only one domain responsible for ligand binding (the C-terminal region) [3], whereas HSA has 2 major binding sites: site I and site II [29], and is one of the main transport proteins. CD analysis was done to verify whether the RTmc-HSA interaction induces changes in albumin secondary structure (Fig.…”

Section: Interaction Of Rtmc With Hsamentioning

confidence: 99%

“…RTmc was also chosen due to its strong antioxidant activity [24][25][26], because it can act against free radicals stress − the second main reason of neurodegenerative disorders [27]. We also experimented with HSA, which is the most abundant protein in blood, with an important role as a transporter of different guest molecules [28,29]. Thus the investigation of RTmc interaction with HSA is essential for estimating how albumin can affect the bioavailability of tannin in biological systems.…”

Section: Introductionmentioning

confidence: 99%

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Interaction of α-synuclein with Rhus typhina tannin – Implication for Parkinson’s disease

Sękowski

Йонов

Abdulladjanova

et al. 2017

Colloids and Surfaces B: Biointerfaces

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The etiology of Parkinson's disease (PD) relates to α-synuclein, a small protein with the ability to aggregate and form Lewy bodies. One of its prevention strategies is inhibition of α-synuclein oligomerization. We have investigated the interaction of α-synuclein and human serum albumin with 3,6-bis-О-di-О-galloyl-1,2,4-tri-О-galloyl-β-d-glucose (a tannin isolated from the plant Rhus typhina). Using fluorescence spectroscopy method we found that this tannin interacts strongly with α-synuclein forming complexes. Circular dichroism analysis showed a time-dependent inhibition of α-synuclein aggregation in the presence of the tannin. On the other hand, 3,6-bis-О-di-О-galloyl-1,2,4-tri-О-galloyl-β-d-glucose had a much stronger interaction with human serum albumin than α-synuclein. The calculated binding constant for tannin-protein interaction was considerably higher for albumin than α-synuclein. This tannin interacted with albumin through a "sphere of action" mechanism. The results lead to the conclusion that 3,6-bis-О-di-О-galloyl-1,2,4-tri-О-galloyl-β-d-glucose is a potent preventive compound against Parkinson's disease. However, this tannin interacts very strongly with human serum albumin, significantly reducing the bioavailability of this compound.

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“…Next, the number of binding sites (n) in HSA and the binding constant (K b ) were calculated using the Hill equation (Eq. (4)) [35] and based on Hill plots presented on Fig. 4 (left panel).…”

Section: Fluorescence Analysis Of Tannin-hsa Interactionsmentioning

confidence: 99%

Influence of valoneoyl groups on the interactions between Euphorbia tannins and human serum albumin

Sękowski

Bitiucki

Йонов

et al. 2018

Journal of Luminescence

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Tannins belonging to plant polyphenols, are large group of compounds with diverse biological activity. Many of them are being studied as potential natural medicine due to their antioxidant, antiviral, antibacterial or anticancer properties. However, so far little is known about the structural and functional relations in protein-tannin interactions, in particularly the role of valoneoyl groups in tannin structure. In this study we first investigated the mechanisms of interaction 1,2-di-O-galloyl-4,6-valoneoyl-β-D-glucose (Tannin 1), 2-O-galloyl-4,6-valoneoylβ-D-glucose (Tannin 2), 3-O-galloyl-1,2-valoneoyl-β-D-glucose (Tannin 3) isolated from Euphorbia plants with human serum albumin (HSA). To get more detailed information about nature of albumin-tannin interactions besides standard Trp fluorescence quenching analysis we used also transmission electron microscopy (TEM), circular dichroism (CD) and fluorescence labelling (ANS dye) techniques. It was shown that all the tannins strongly interacted with HSA and quenched the tryptophan amino acid (Trp) fluorescence but slightly changed protein secondary structure (circular dichroism CD analysis). TEM demonstrated that all used compounds formed complexes with HSA. Tannin 3 most strongly quenched HSA fluorescence and changed protein dynamic as well as had the highest binding constant (12.4 ± 1.1 × 10 13 M −1 s −1 in comparison with 7.0 ± 0.38 × 10 13 M −1 s −1 for tannin 1 and 8.6 ± 1.1 × 10 13 M −1 s −1 for tannin 2). For tannin 1 that was the largest of the studied compounds was observed the weakest influence on the fluorescence parameters, probably due to the effect of steric hindrance limiting interaction with albumin Trp pocket. On the other hand T1 induced the strongest changed secondary structure of HSA in comparison to another studied tannins. Our results demonstrated that all used tannins interact with albumin by complex formation but in the manner depends on chemical structure and flexibility of studied compounds.

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In vitro study on the interaction of methoxyflurane with human serum albumin: Phenotypic characterization

Cited by 8 publications

References 34 publications

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

Interaction of α-synuclein with Rhus typhina tannin – Implication for Parkinson’s disease

Influence of valoneoyl groups on the interactions between Euphorbia tannins and human serum albumin

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