Binding mechanism and antioxidant activity of piperine to hemoglobin

Hu, Xia; Wu, Di; Tang, Lan; Zhang, Jing; Zeng, Zhen; Geng, Fang; Li, Hui

doi:10.1016/j.foodchem.2022.133558

Cited by 32 publications

(24 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The binding of PIP to Mb was more stable compared to previous studies on the interaction of tetrameric protein Hb with PIP. 20 These results suggest that PIP affects the conformation of Mb and may be responsible for the enhanced antioxidant activity of the Mb–PIP complex systems. These findings indicate that the binding of PIP influences the conformation of Mb.…”

Section: Resultsmentioning

confidence: 88%

Binding behavior and antioxidant study of spice extract piperine with respect to meat myoglobin

Cai

et al. 2023

Food Funct.

Self Cite

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 88%

Binding behavior and antioxidant study of spice extract piperine with respect to meat myoglobin

Cai

et al. 2023

Food Funct.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Consequently, albumin seemed to affect the difference in the cellular uptake between Toc and T3. Hence, we analyzed the affinity of Toc and T3 to albumin by fluorescence spectroscopy and a computational molecular docking approach 30 – 36 . As a result, we found that Toc and T3 demonstrate different affinities to albumin, and this difference might have induced the difference in their cellular uptake.…”

Section: Introductionmentioning

confidence: 99%

The difference in the cellular uptake of tocopherol and tocotrienol is influenced by their affinities to albumin

Nakatomi

Itaya-Takahashi

Horikoshi

et al. 2023

Sci Rep

View full text Add to dashboard Cite

Vitamin E is classified into tocopherol (Toc) and tocotrienol (T3) based on its side chains. T3 generally has higher cellular uptake than Toc, though the responsible mechanism remains unclear. To elucidate this mechanism, we hypothesized and investigated whether serum albumin is a factor that induces such a difference in the cellular uptake of Toc and T3. Adding bovine serum albumin (BSA) to serum-depleted media increased the cellular uptake of T3 and decreased that of Toc, with varying degrees among α-, β-, γ-, and δ-analogs. Such enhanced uptake of α-T3 was not observed when cells were incubated under low temperature (the uptake of α-Toc was also reduced), suggesting that Toc and T3 bind to albumin to form a complex that results in differential cellular uptake of vitamin E. Fluorescence quenching study confirmed that vitamin E certainly bound to BSA, and that T3 showed a higher affinity than Toc. Molecular docking further indicated that the differential binding energy of Toc or T3 to BSA is due to the Van der Waals interactions via their side chain. Overall, these results suggested that the affinity of Toc and T3 to albumin differs due to their side chains, causing the difference in their albumin-mediated cellular uptake. Our results give a better mechanistic insight into the physiological action of vitamin E.

show abstract

“…Sometimes, it is worthwhile to know. The interaction either is cooperative or competitive if the stoichiometry of the binder to HSA is more than one 22 …”

Section: Introductionmentioning

confidence: 99%

“…The interaction either is cooperative or competitive if the stoichiometry of the binder to HSA is more than one. 22 Aldehyde dehydrogenases (ALDHs) is a family of multifunctional NAD(P) + -dependent group of phase I detoxification enzyme systems entailed for the irreversible oxidation of a wide variety of biogenic and xenogenic aldehydic compounds to their corresponding carboxylic acids. 23 This reaction is for the ultimate relief of aldehydic stress.…”

mentioning

confidence: 99%

Human serum albumin subdomain IB is physiologically adapted for payloading homopterocarpin to human aldehyde dehydrogenase: Combinatorial in vitro and in silico approaches

Ayenero,

Akinwusi,

Kolawole

et al. 2023

J of Molecular Recognition

View full text Add to dashboard Cite

The in vitro interactions of homopterocarpin, a potent antioxidant and anti‐ulcerative isoflavonoid, with human serum albumin (HSA) and human aldehyde dehydrogenase (hALDH) were explored using various spectroscopic methods, in silico and molecular dynamic (MD) studies. The result showed that homopterocarpin quenched the intrinsic fluorescences of HSA and hALDH. The interactions were entropically favorable, driven primarily by hydrophobic interactions. The proteins have one binding site for the isoflavonoid. This interaction increased the proteins hydrodynamic radii by over 5% and caused a slight change in HSA surface hydrophobicity Homopterocarpin preferentially binds to HSA subdomain IB with a binding affinity of −10.1 kcal/mol before interaction stoke with hALDH (–8.4 kcal/mol). HSA‐homopterocarpin complex attained pharmacokinetic‐pharmacodynamics reversible equilibration time faster than ALDH‐homopterocarpin. However, the probable and eventual therapeutic effect of homopterocarpin is the mixed inhibition ALDH activity having a Ki value of 20.74 μM. The MD results revealed the stabilization of the complex in HSA–homopterocarpin and ALDH–homopterocarpin from their respective spatial structures of the complex. The findings of this research will provide significant benefits in understanding the pharmacokinetics characteristics of homopterocarpin at the clinical level.

show abstract

Binding mechanism and antioxidant activity of piperine to hemoglobin

Cited by 32 publications

References 40 publications

Binding behavior and antioxidant study of spice extract piperine with respect to meat myoglobin

Binding behavior and antioxidant study of spice extract piperine with respect to meat myoglobin

The difference in the cellular uptake of tocopherol and tocotrienol is influenced by their affinities to albumin

Human serum albumin subdomain IB is physiologically adapted for payloading homopterocarpin to human aldehyde dehydrogenase: Combinatorial in vitro and in silico approaches

Contact Info

Product

Resources

About