Fluorescence studies by quenching and protein unfolding on the interaction of bioactive compounds in water extracts of kiwi fruit cultivars with human serum albumin

Park, Yong Seo; Polovka, Martin; Martínez-Ayala, Alma Leticia; González‐Aguilar, Gustavo A.; Ham, Kyung‐Sik; Kang, Seong‐Gook; Park, Yang-Kyun; Heo, Buk-Gu; Namieśnik, Jacek; Gorinstein, Shela

doi:10.1016/j.jlumin.2014.11.044

Cited by 17 publications

(3 citation statements)

References 30 publications

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“…Tannic and caffeic acids and quercetin were also compared with the natural fibrinogen. Few studies of the roles played by different phenolic fractions in wine astringency using methods involving fluorescence spectra are available [26]. However, the polymeric proanthocyanidins were found to possess higher activity than the other fractions.…”

Section: Binding Properties Of Wines and Some Phenolic Compounds With The Main Human Proteinsmentioning

confidence: 99%

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

Shafreen¹,

Lakshmi

Pandian

et al. 2021

Molecules

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Previous reports have shown that consumption of wine has several health benefits; however, there are different types of wine. In the present study, red wines were investigated for their compositions of active ingredients. The interaction of each component in terms of its binding mode with different serum proteins was unraveled, and the components were implicated as drug candidates in clinical settings. Overall, the study indicates that red wines have a composition of flavonoids, non-flavonoids, and phenolic acids that can interact with the key regions of proteins to enhance their biological activity. Among them, rutin, resveratrol, and tannic acid have shown good binding affinity and possess beneficial properties that can enhance their role in clinical applications.

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Section: Binding Properties Of Wines and Some Phenolic Compounds With The Main Human Proteinsmentioning

confidence: 99%

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

Shafreen¹,

Lakshmi

Pandian

et al. 2021

Molecules

Self Cite

View full text Add to dashboard Cite

show abstract

“…Conversely, a weak binding efcacy of a drug may be associated with a shorter half-life and early excretion from the body, thus making it less-efective owing to its shortage at the desired site of action. Moreover, the binding of substances, which are obtained from natural sources (plants), to serum albumin has greatly captivated the interests of researchers [16][17][18][19][20][21][22][23][24][25]. Recently, the bindings of several natural products that were obtained from diferent sources, including Red sea sponge, mountain thyme, cuminol, and safron, to serum albumins were investigated, and it was observed that these compounds interacted diferently with serum albumin and exerted diferent efects on the structure of the latter [26][27][28][29].…”

Section: Introductionmentioning

confidence: 99%

Study of the Binding of Cuminaldehyde with Bovine Serum Albumin by Spectroscopic and Molecular Modeling Methods

Ali

Rehman

Al‐Lohedan

et al. 2023

Journal of Spectroscopy

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Here, we investigated the interaction of cuminaldehyde with a model carrier protein, bovine serum albumin (BSA). The formation of the BSA–cuminaldehyde complex was confirmed through ultraviolet–visible (UV–Vis) spectroscopy and further proven by detailed intrinsic fluorescence spectroscopic measurements. As observed, cuminaldehyde quenched the intrinsic tryptophanyl fluorescence of BSA. The fluorescence data, before the analyses, were corrected for the inner filter effect (IFE) because of the significant absorption of cuminaldehyde at the excitation wavelength that was employed in the measurements. The typical Stern–Volmer plots were slightly nonlinear; they exhibited negative deviation toward the x-axis, a typical phenomenon that is observed with proteins possessing more than one tryptophan residue. Thus, the modified Stern–Volmer equation was employed to analyze the data. The analyzed data revealed that the interaction of cuminaldehyde with BSA proceeded via a static quenching mechanism and that there was a fair 1 : 1 binding between them. The interaction was strengthened by hydrophobic forces and hydrogen bonding. A lowered concentration of cuminaldehyde did not affect the secondary structure of BSA, although an increased one partially exposed the protein by decreasing its α-helical contents. The molecular dockings and simulations of BSA and cuminaldehyde further confirmed the formation of the stable BSA–cuminaldehyde complex. The in silico results also revealed that the contributions of the hydrophobic interaction and hydrogen bonding were the driving forces that imparted the stability.

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“…These compounds are of considerable interest because of a variety of their biological activities, e.g., anticancer [1], antitubercular [2], antibacterial [3], antifungal [4], anti-HIV [5], analgesic [6] and Human serum albumin (HSA), which is the main protein in human blood plasma, plays a pivotal role in the pharmacodynamic and pharmacokinetic properties because it can not only serve as a carrier for drugs, but also can participate in drug absorption, distribution and metabolism [10][11][12][13][14][15]. Interaction studies of HSA with biological molecules can elucidate the properties of the drug-protein complex because they may provide useful information about the structural features that determine the therapeutic effectiveness of drugs.…”

Section: Introductionmentioning

confidence: 99%

Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy

et al. 2017

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Abstract:The interactions of dihydroquinazolines with human serum albumin (HSA) were studied in pH 7.4 aqueous solution via fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopic techniques. In this work, 6-chloro-1-(3,3-dimethyl-butanoyl)-2-(un)substitutedphenyl-2,3-dihydroquinazolin-4(1H)-one (PDQL) derivatives were designed and synthesized to study the impact of five similar substituents (methyl, methoxy, cyano, trifluoromethyl and isopropyl) on the interactions between PDQL and HSA using a comparative methodology. The results revealed that PDQL quenched the intrinsic fluorescence of HSA through a static quenching process. Displacement experiments with site-specific markers revealed that PDQL binds to HSA at site II (subdomain IIIA) and that there may be only one binding site for PDQL on HSA. The thermodynamic parameters indicated that hydrophobic interactions mainly drove the interactions between PDQL and HSA. The substitution using five similar groups in the benzene ring could increase the interactions between PDQL and HSA to some extent through the van der Waals force or hydrogen bond effects in the proper temperature range. Isopropyl substitution could particularly enhance the binding affinity, as observed via comparative studies.

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Fluorescence studies by quenching and protein unfolding on the interaction of bioactive compounds in water extracts of kiwi fruit cultivars with human serum albumin

Cited by 17 publications

References 30 publications

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

Study of the Binding of Cuminaldehyde with Bovine Serum Albumin by Spectroscopic and Molecular Modeling Methods

Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy

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