Structural basis and anticancer properties of ruthenium-based drug complexed with human serum albumin

Zhang, Yao; Ho, A.S.H.; Yue, Jiping; Kong, Linlin; Zhou, Zuping; Wu, Xiaoyang; Yang, Feng; Liang, Hong

doi:10.1016/j.ejmech.2014.08.071

Cited by 62 publications

(44 citation statements)

References 47 publications

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“…Based on the structure of HSA–Cu(BpT)Br complex, Cu(BpT)Br binds to the IIA sub-domain of HSA by His146 specific coordinated with Cu center. However, Ru agents may bind to the IB and/or IIA sub-domain(s) of HSA because the binding site and binding mode of metal agents to IIA sub-domain depend on their molecular structure (Webb et al., 2013 ; Zhang et al., 2014 ; Ferraro et al., 2015 ). Therefore, the optimal strategy for HSA delivering two metal agents is that Cu(BpT)Br and NAMI-A bind to the IIA and IB sub-domains of HSA, respectively.…”

Section: Discussionmentioning

confidence: 99%

HSA-based multi-target combination therapy: regulating drugs’ release from HSA and overcoming single drug resistance in a breast cancer model

Gou

Zhang

et al. 2018

Drug Delivery

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Multi-drug delivery systems, which may be promising solution to overcome obstacles, have limited the clinical success of multi-drug combination therapies to treat cancer. To this end, we used three different anticancer agents, Cu(BpT)Br, NAMI-A, and doxorubicin (DOX), to build human serum albumin (HSA)-based multi-drug delivery systems in a breast cancer model to investigate the therapeutic efficacy of overcoming single drug (DOX) resistance to cancer cells in vivo, and to regulate the drugs’ release from HSA. The HSA complex structure revealed that NAMI-A and Cu(BpT)Br bind to the IB and IIA sub-domain of HSA by N-donor residue replacing a leaving group and coordinating to their metal centers, respectively. The MALDI-TOF mass spectra demonstrated that one DOX molecule is conjugated with lysine of HSA by a pH-sensitive linker. Furthermore, the release behavior of three agents form HSA can be regulated at different pH levels. Importantly, in vivo results revealed that the HSA–NAMI-A–Cu(BpT)Br–DOX complex not only increases the targeting ability compared with a combination of the three agents (the NAMI-A/Cu(BpT)Br/DOX mixture), but it also overcomes DOX resistance to drug-resistant breast cancer cell lines.

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Section: Discussionmentioning

confidence: 99%

HSA-based multi-target combination therapy: regulating drugs’ release from HSA and overcoming single drug resistance in a breast cancer model

Gou

Zhang

et al. 2018

Drug Delivery

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“…Delivery of some other drugs such as HI 6 dichloride monohydrate and HI 6 dimethane sulfonate (treatment of intoxication by organophosphorus [OP]) [110], aspirin [111], methotrexate (anticancer drug) [112], platinum (IV) prodrugs such as cisplatin (treatment of cancer) [35], ruthenium-based anticancer drugs [113], diclofenac (an anti-inflammatory drug), and tacrolimus (as a immunosuppressant) [41] have also been investigated to improve their stability and solubility.…”

Section: Albumin Conjugates For Drug Deliverymentioning

confidence: 99%

Albumin nanostructures as advanced drug delivery systems

Karimi

Bahrami

Ravari

et al. 2016

Expert Opinion on Drug Delivery

331

190

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Introduction One of the biggest impacts that the nanotechnology has made on medicine and biology, has been in the area of drug delivery systems (DDSs). Many drugs suffer from serious problems concerning insolubility, instability in biological environments, poor uptake into cells and tissues, suboptimal selectivity for targets and unwanted side effects. Nanocarriers can be designed as DDSs to overcome many of these drawbacks. One of the most versatile building blocks to prepare these nanocarriers is the ubiquitous, readily available and inexpensive protein, serum albumin. Areas covered This review covers the use of different types of albumin (human, bovine, rat, and chicken egg) to prepare nanoparticle and microparticle-based structures to bind drugs. Various methods have been used to modify the albumin structure. A range of targeting ligands can be attached to the albumin that can be recognized by specific cell receptors that are expressed on target cells or tissues. Expert opinion The particular advantages of albumin used in DDSs include ready availability, ease of chemical modification, good biocompatibility, and low immunogenicity. The regulatory approvals that have been received for several albumin-based therapeutic agents suggest that this approach will continue to be successfully explored.

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“…These peculiarities of ruthenium complexes can be partly explained by the ability of ruthenium to imitate iron in biological media, as well as by its rich coordination chemistry from the standpoint of available oxidative states, hydrolysis rates, and photochemistry. [106][107][108][109][110][111][112][113]…”

Section: Metal Complexesmentioning

confidence: 99%

Supramolecular interaction of transition metal complexes with albumins and DNA: Spectroscopic methods of estimation of binding parameters

Galkina

Проскурнин

2018

Applied Organom Chemis

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Binding parameters of metal complexes with albumins and DNA since the middle of 1990s are considered and summarized. The most widespread spectroscopic methods of estimation of binding parameters are discusseddirect fluorescent methods, indirect fluorescent methods (by fluorescence quenching parameters), and ways of estimation of binding constants by other optical spectroscopic methods. The methods and approaches to calculations used for the determination of binding constants are discussed. The data on the already found binding constants and kinetic parameters is systematized.KEYWORDS albumins, DNA, metal complexes, proteins, supramolecular interaction Funding information: Russian Foundation for Basic Research, Grant/Award Number: 16-03-01089_a 16-53-50027_YaF_a Abbreviations and designations used: F 0 , fluorescence intensity in the absence of a quencher; F, fluorescence intensity in the presence of a acid); NTSC, a new thiosemicarbazone; o-cbiaH, 5-(2-carboxybenzyloxy)isophthalic acid; o-van-gln, a Schiff base derived from o-vanillin and glutamine; o-van-L-met, Schiff base derived from o-vanillin and L-methionine; oxo, 5-

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Structural basis and anticancer properties of ruthenium-based drug complexed with human serum albumin

Cited by 62 publications

References 47 publications

HSA-based multi-target combination therapy: regulating drugs’ release from HSA and overcoming single drug resistance in a breast cancer model

HSA-based multi-target combination therapy: regulating drugs’ release from HSA and overcoming single drug resistance in a breast cancer model

Albumin nanostructures as advanced drug delivery systems

Supramolecular interaction of transition metal complexes with albumins and DNA: Spectroscopic methods of estimation of binding parameters

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