Formation of a Multiligand Complex of Bovine Serum Albumin with Retinol, Resveratrol, and (−)-Epigallocatechin-3-gallate for the Protection of Bioactive Components

Wu, Yi; Cheng, Hao; Chen, Yantao; Chen, Lingyun; Fang, Zheng; Liang, Li

doi:10.1021/acs.jafc.7b00326

Cited by 58 publications

(84 citation statements)

References 40 publications

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“…Three homologous domains build up BSA, which is called as domain I, II, and III. Each domain is divided into two subdomains (A and B) [1,2].…”

Section: Introductionmentioning

confidence: 99%

“…BSA has been widely used as drug delivery device because of its non-toxicity, biodegradability, nonimmunogenicity, water solubility, availability and its low cost, because large quantities of it can be readily purified from bovine blood [3]. In order to be used as drug delivery device, BSA has been bound with ligand complex [1] and polymer [4], or complexed with magnetic iron oxide [5].…”

Section: Introductionmentioning

confidence: 99%

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pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

Patriati

Putra

2021

Jurnal Teknologi

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The pH-dependent structures of the bovine serum albumin (BSA), under physiological conditions that permit enzymatic activity, were investigated by small-angle neutron scattering (SANS). The unfolding behavior of BSA in solution is important to understand the mechanism of protein aggregation due to protein conformational change. The information of protein structure is crucial to design the perfect protein-based drug delivery device. This information will be useful as a complementary data of BSA crystal structure in static state. The structure of BSA in solution was found to be heart shaped, nearly identical to bovine serum albumin crystal structure. The globular heart shaped structure of BSA was still maintained at alkaline pH range of 7 to 11. It underwent partial unfolding at pH 5 and continued to unfold at pH 3. The unfolded-structure of BSA shows that the globular structure started to change into a cylinder-like structure at pH 3 which was clearly shown in Kratky plot. These results were confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIF in obtaining the three-dimensional protein structure model.

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“…Three homologous domains build up BSA, which is called as domain I, II, and III. Each domain is divided into two subdomains (A and B) [1,2].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

Patriati

Putra

2021

Jurnal Teknologi

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“…Combinations of different antioxidants have the potential to reduce the toxicity or pro‐oxidation of bioactive compounds delivered at high doses. However, such combinations may give rise to antagonistic, additive or synergistic effects on the bioactivity and stability of the compounds (Wang et al ., 2011; Wu et al ., 2017). It is important to identify such interactions and their mechanisms in order to facilitate the formulation of high‐quality functional products.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant activity and stability of α‐tocopherol, resveratrol and epigallocatechin‐3‐gallate in mixture and complexation with bovine serum albumin

Dong

Yin

Wusigale

et al. 2020

Int J of Food Sci Tech

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Intermolecular interactions among α‐tocopherol, resveratrol and EGCG appear to be antagonistic based on antioxidant activity but improve their structural stability and preserve antioxidant property. These bioactive compounds interact with BSA to form tri‐ligand complexes. Such tri‐ligand complexes maintain structural integrity and antioxidant property of a‐tocopherol, resveratrol and EGCG simultaneously and to a greater degree than is observed for mono‐ligand complexes with BSA.

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“…A few studies have demonstrated that EGCg competes with 5-fluorouracil and related drugs for binding sites on serum albumin [30,33]. However, EGCg, resveratrol, and retinol simultaneously bind serum albumin at unique binding sites with minimal structural or chemical cross-talk between the ligands [34]. A knowledge gap that limits exploitation of the pharmaceutical potential of EGCg is poor understanding of how natural endogenous ligands of serum albumin combined with exogenous ligands such as EGCg affect the protein.…”

Section: Introductionmentioning

confidence: 99%

Conformation and Aggregation of Human Serum Albumin in the Presence of Green Tea Polyphenol (EGCg) and/or Palmitic Acid

2019

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Polyphenols such as epigallocatechin gallate (EGCg) may have roles in preventing some chronic diseases when they are ingested as components of plant-based foods and beverages. Human serum albumin (HSA) is a multi-domain protein that binds various ligands and aids in their transport, distribution, and metabolism in the circulatory system. In the present study, the HSA-EGCg interaction in the absence or presence of fatty acid has been investigated. Förster resonance energy transfer (FRET) was used to determine inter- and intra-domain distances in the protein with and without EGCg and palmitic acid (PA). By labeling Cys-34 with 7-(diethyl amino)-4-methylcoumarin 3-maleimide (CPM), the distance between Trp-214 at domain IIA and CPM-Cys-34 at domain IA could be established. A small amount of PA decreased the distance, while a large amount increased the distance up to 5.4 Å. EGCg increased the inter-domain distance in HSA and HSA-PA up to 2.8 and 7.6 Å, respectively. We concluded that PA affects protein conformation more significantly compared to EGCg. Circular dichroism (CD) established that EGCg affects protein secondary structure more significantly than PA. PA had little effect on the α-helix content of HSA, while EGCg decreased the α-helix content in a dose-dependent fashion. Moreover, EGCg decreased α-helix content in HSA and HSA-PA to the same level. Dynamic light scattering (DLS) data revealed that both PA and EGCg increased HSA aggregation. EGCg increased HSA aggregation more significantly and promoted formation of aggregates that were more heterogenous. Any of these effects could impact the ability of serum albumin to transport and stabilize ligands including EGCg and other polyphenols.

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Formation of a Multiligand Complex of Bovine Serum Albumin with Retinol, Resveratrol, and (−)-Epigallocatechin-3-gallate for the Protection of Bioactive Components

Cited by 58 publications

References 40 publications

pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

Antioxidant activity and stability of α‐tocopherol, resveratrol and epigallocatechin‐3‐gallate in mixture and complexation with bovine serum albumin

Conformation and Aggregation of Human Serum Albumin in the Presence of Green Tea Polyphenol (EGCg) and/or Palmitic Acid

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