Interaction of curcumin with intravenous immunoglobulin: A fluorescence quenching and Fourier transformation infrared spectroscopy study

Yang, Zhenle; Du, Juan; Yao, Xiaojun; Lei, Ruixia; Zheng, Xudong; Liu, Jianning; Hu, Huaisheng; Li, Hong

doi:10.1016/j.imbio.2008.02.003

Cited by 44 publications

(19 citation statements)

References 38 publications

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“…The magnitude of the binding constants for the association of curcumin to HSA and IgG agree with the values obtained in previous studies. 22,26,34 Here, we report the binding constants for the association of curcumin to fibrinogen and transferrin for the first time, which have values of (5.99 ( 1.75) Â 10 4 and (5. 15 ( 1.05) Â 10 3 M -1 , respectively.…”

Section: Resultsmentioning

confidence: 92%

Effective Stabilization of Curcumin by Association to Plasma Proteins: Human Serum Albumin and Fibrinogen

2009

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The use of curcumin as an effective wound healing agent is of significant interest currently. It is well established that curcumin undergoes rapid degradation in physiological buffer by hydrolysis. The means by which curcumin is stabilized at the wound site to enable healing is poorly understood because blood plasma is composed of approximately 92% water. Plasma proteins, which constitute the remaining 6-8%, has been shown to stabilize curcumin. It is, however, still unclear which proteins are responsible for this phenomenon. In this study, the effects of major plasma proteins, which include human serum albumin (HSA), fibrinogen, immunoglobulin G (IgG), and transferrin, on stabilizing curcumin are investigated. In particular, we investigate their effects on the hydrolysis of curcumin at pH 7.4. In the presence of both transferrin and IgG, curcumin continues to undergo rapid hydrolysis but this reaction is suppressed by the presence of either HSA or fibrinogen with an impressive yield of approximately 95%. Furthermore, the binding constants of curcumin to HSA and fibrinogen are on the order of 10(4) and 10(5) M(-1), respectively. The binding constants of transferrin and IgG, however, are at least 1 order of magnitude less than those of HSA and fibrinogen. The results support that strong binding occurs at the hydrophobic moieties of HSA and fibrinogen, excluding water access. Therefore, strong interactions with HSA and fibrinogen inhibit hydrolysis of curcumin and in turn lead to effective suppression of degradation.

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Section: Resultsmentioning

confidence: 92%

Effective Stabilization of Curcumin by Association to Plasma Proteins: Human Serum Albumin and Fibrinogen

2009

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“…Although CCM has been shown to exhibit many bioactivities such as antioxidant, anti-inflammatory, anticancer and various malignant diseases, it is extremely limited in its application due to its low bioavailability related to its insolubility in water as well as its poor absorption and rapid metabolism (Aggarwal, Sundaram, Malani, & Ichikawa, 2007;Anand, Kunnumakkara, Newman, & Aggarwal, 2007;Anand, Sundaram, Jhurani, Kunnumakkara, & Aggarwal, 2008). Attempts to improve the bioavailability of CCM have been reported by making complexes with carriers, such as bovine serum albumin (Bourassa, Kanakis, Tarantilis, Pollissiou, & Tajmir-Riahi, 2010), human serum albumin (Mandeville, Froehlich, & Tajmir-Riahi, 2009;Zsila, Bikadi, & Simonyi, 2003), b-lactoglobulin (Mohammadi, Bordbar, Divsalar, Mohammadi, & Saboury, 2009;Sneharani, Karakkat, Singh, & Rao, 2010), immunoglobulin (Liu et al, 2008), chitosan (Shelma & Sharma, 2010), phospholipids (Liu, Lou, Zhao, & Fan, 2006) or by formation of liposomes (Li, Braiteh, & Kurzrock, 2005), micelles (Sahu, Kasoju, & Bora, 2008) and encapsulation or nanoparticles (Bisht et al, 2007;Shaikh, Ankola, Beniwal, Singh, & Kumar, 2009;Wang et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Absorption mechanism of whey-protein-delivered curcumin using Caco-2 cell monolayers

Cui

Ngadi

et al. 2015

Food Chemistry

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“…All of the current values of K q for ligands and Ho(III) complexes are much greater than that of K q(max) (2.0 Â 10 10 M À1 s -1 ), the maximum quenching rate constant of bimolecular diffusion collision, which are indicative of static types of quenching mechanisms arisen from the formations of dark complexes between the fluorophores and quenching agents [44,45]. It is reported that the loss of fluorescence intensity at the maximum wavelength indicates the displacement of EtBr from DNA-EtBr complex by a compound and the intercalative binding between the compound with DNA [34].…”

Section: Dna-etbr Quenching Assaymentioning

confidence: 88%

Synthesis, crystal structure, antioxidation and DNA binding properties of binuclear Ho(III) complexes of Schiff-base ligands derived from 8-hydroxyquinoline-2-carboxyaldehyde and four aroylhydrazines

Zhou

2009

Journal of Organometallic Chemistry

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Interaction of curcumin with intravenous immunoglobulin: A fluorescence quenching and Fourier transformation infrared spectroscopy study

Cited by 44 publications

References 38 publications

Effective Stabilization of Curcumin by Association to Plasma Proteins: Human Serum Albumin and Fibrinogen

Effective Stabilization of Curcumin by Association to Plasma Proteins: Human Serum Albumin and Fibrinogen

Absorption mechanism of whey-protein-delivered curcumin using Caco-2 cell monolayers

Synthesis, crystal structure, antioxidation and DNA binding properties of binuclear Ho(III) complexes of Schiff-base ligands derived from 8-hydroxyquinoline-2-carboxyaldehyde and four aroylhydrazines

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