Binding of daunorubicin to human serum albumin using molecular modeling and its analytical application

Cui, Fengling; Qin, Lixia; Zhang, Guisheng; Yao, Xiaojun; Du, Juan

doi:10.1016/j.ijbiomac.2007.10.013

Cited by 29 publications

(9 citation statements)

References 36 publications

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“…It has an important role in maintaining the colloidal osmotic pressure in blood. It also transports and distributes exogenous and endogenous substances, such as nutrients, hormones, fatty acids and many diverse drugs [8,9]. HSA is a globular protein consisting of 585 amino acid residues and considered to have three specific binding sites (labeled as I-III) [10].…”

Section: Introductionmentioning

confidence: 99%

Interaction of the docetaxel with human serum albumin using optical spectroscopy methods

Cheng

Liu

Zhang

et al. 2009

Journal of Luminescence

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Section: Introductionmentioning

confidence: 99%

Interaction of the docetaxel with human serum albumin using optical spectroscopy methods

Cheng

Liu

Zhang

et al. 2009

Journal of Luminescence

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“…Prior to in vivo assays or therapeutic use, it would be interesting to assess the behavior of DIDS in the presence of the most abundant protein in blood plasma, human serum albumin (HSA). Indeed, it has been shown that the distribution, the available concentration and the metabolism of numerous drugs can be significantly altered by their binding to HSA [13].…”

Section: Introductionmentioning

confidence: 99%

“…HSA shares about 80 percent of sequence similarity with bovine serum albumin (BSA). Both proteins have three domains (I, II and III), each composed of two subdomains, A and B [13].…”

Section: Introductionmentioning

confidence: 99%

Interactions of the Rad51 inhibitor DIDS with human and bovine serum albumins: Optical spectroscopy and isothermal calorimetry approaches

et al. 2019

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Rad51 is a key protein in DNA repair by homologous recombination and an important target for development of drugs in cancer therapy. 4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) has been used in clinic during the past 30 years as an inhibitor of anion transporters and channels. DIDS has been demonstrated to affect Rad51-mediated homologous pairing and strand exchange, key processes in homologous recombination. Consequently, DIDS has been considered as a potential revertant of radio-and chemo-resistance of cancer cells, the major causes of therapy failure. Here, we have investigated the behavior of DIDS towards serum albumins. The effects of environmental factors, primarily, solvent polarity, on DIDS stability were evaluated, and the mechanisms of interaction of DIDS with human or bovine serum albumin were analyzed using isothermal calorimetry, circular dichroism and fluorescence spectroscopies. DIDS interaction with both serum albumins have been demonstrated, and the interaction characteristics have been determined. By comparing these characteristics for several DIDS derivatives, we have identified the DIDS moiety essential for the interaction. Furthermore, site competition data indicate that human albumin has two DIDS-binding sites: a high-affinity site in the IIIA subdomain and a low-affinity one in the IB subdomain. Molecular docking has revealed the key molecular moieties of DIDS responsible for its interactions in each site and shown that the IB site can bind two ligands. These findings show that binding of DIDS to serum albumin may change the balance between the free and bound DIDS forms, thereby affecting its bioavailability and efficacy against Rad51.

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“…On the other side, the studies on this aspect can provide information of the structural features that determine the therapeutic effectivity of drugs and have been an interesting research field in life sciences, chemistry, and clinical medicine. Recently, there have been some papers devoted to studies of the interaction between drugs and proteins by fluorescence spectroscopy [4,5], yet the investigation on the binding interaction of DNR and cardiac myosin (CM) has not been reported, which typically involved in bovine serum albumin (BSA) and human serum albumin [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Effect of Zinc and Copper on the Interaction of Daunorubicin with Cardiac Myosin

Liu

Lin

Sun

et al. 2008

Biol Trace Elem Res

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Daunorubicin (DNR) is an anthracyline antibiotic which induces a well-described but incompletely understood cardiac toxicity. In this study, a direct action of DNR on the major contractile protein, cardiac myosin (CM), was described utilizing the fluorescence spectroscopy. The quenching mechanism was suggested to be static quenching according to the fluorescence measurement. In particular, the effects of common ions on the binding constants of DNR with CM were also investigated under physiological conditions, and the quenching constant K(SV) and binding constant K(LB) were obtained at room temperature. These data proved that Zn2+ and/or Cu2+ potentiated quenching fluorescence intensity of DNR-CM complex. Moreover, the normal ratio of Zn2+ to Cu2+ was able to competitively inhibit the binding interaction of DNR with CM, which might contribute to exert the most significant cardioprotective effect and guarantee the contractile machinery of cardiac muscle.

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Binding of daunorubicin to human serum albumin using molecular modeling and its analytical application

Cited by 29 publications

References 36 publications

Interaction of the docetaxel with human serum albumin using optical spectroscopy methods

Interaction of the docetaxel with human serum albumin using optical spectroscopy methods

Interactions of the Rad51 inhibitor DIDS with human and bovine serum albumins: Optical spectroscopy and isothermal calorimetry approaches

Effect of Zinc and Copper on the Interaction of Daunorubicin with Cardiac Myosin

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