Probing the binding interaction of human serum albumin with three bioactive constituents of Eriobotrta japonica leaves: Spectroscopic and molecular modeling approaches

Wang, Qing; Sun, Qiaomei; Ma, Xiaodong; Rao, Zaisheng; Li, Hui

doi:10.1016/j.jphotobiol.2015.04.030

Cited by 18 publications

(9 citation statements)

References 35 publications

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“…1a), a pentacyclic triterpene compound, is one of the lipophilic constituents extracted from the leaves of Eriobotrta japonica [16], the fruit of Cratoegus pinnatifida var. psilosa [17] and the root of Actinidia chinensis [18] and has shown excellent effects against diabetes on animal experiments and clinical trials [19].…”

Section: Introductionmentioning

confidence: 99%

Corosolic acid, a natural triterpenoid, induces ER stress-dependent apoptosis in human castration resistant prostate cancer cells via activation of IRE-1/JNK, PERK/CHOP and TRIB3

Zhang

Wang

et al. 2018

J Exp Clin Cancer Res

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BackgroundThe development of potent non-toxic chemotherapeutic drugs against castration resistant prostate cancer (CRPC) remains a major challenge. Corosolic acid (CA), a natural triterpenoid, has anti-cancer activity with limited side effects. However, CA anti-prostate cancer activities and mechanisms, particularly in CRPC, are not clearly understood. In this study, we investigated CA anti-tumor ability against human CRPC and its mechanism of action.MethodsThe cell apoptosis and proliferation effects were evaluated via MTT detection, colony formation assay and flow cytometry. Western blot, gene transfection and immunofluorescence assay were applied to investigate related protein expression of Endoplasmic reticulum stress. A xenograft tumor model was established to investigate the inhibitory effect of CA on castration resistant prostate cancer in vivo.ResultsThe results showed that CA inhibited cell growth and induced apoptosis in human prostate cancer cell (PCa) line PC-3 and DU145, as well as retarded tumor growth in a xenograft model, exerting a limited toxicity to normal cells and tissues. Importantly, CA activated endoplasmic reticulum (ER) stress-associated two pro-apoptotic signaling pathways, as evidenced by increased protein levels of typical ER stress markers including IRE-1/ASK1/JNK and PERK/eIF2α/ATF4/CHOP. IRE-1, PERK or CHOP knockdown partially attenuated CA cytotoxicity against PCa cells. Meanwhile, CHOP induced expression increased Tribbles 3 (TRIB3) level, which lead to AKT inactivation and PCa cell death. CHOP silencing resulted in PCa cells sensitive to CA-induced apoptosis.ConclusionOur data demonstrated, for the first time, that CA might represent a novel drug candidate for the development of an anti-CRPC therapy.Electronic supplementary materialThe online version of this article (10.1186/s13046-018-0889-x) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Corosolic acid, a natural triterpenoid, induces ER stress-dependent apoptosis in human castration resistant prostate cancer cells via activation of IRE-1/JNK, PERK/CHOP and TRIB3

Zhang

Wang

et al. 2018

J Exp Clin Cancer Res

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“…During docking, NETA/NET was freshly prepared, and CHARMm was added as the force field. Heating and cooling steps were established as described as in a previous study (Wang et al ., 2015, 2015). According to the − CDOCKER energy (−ECD, kcal mol −1 ) ranking, 10 molecular docking poses were saved for each site.…”

Section: Resultsmentioning

confidence: 92%

“…These characteristics may lead to NET‐EN competition with NETA being stronger than the two other components; thus, NET‐EN binds to HSA more easily than NETA. The previous study (Wang et al ., 2015, 2015) indicated that the PPB level of NETA is 1 (binding is >90% [flagged at 90% or AlogP98 > 4.0]), whereas that of NET‐EN is 2 (binding was >95% [flagged at 95% or AlogP98 > 5.0]). Hence, NETA is more likely to be weakly bound to HSA in the blood than NET‐EN.…”

Section: Resultsmentioning

confidence: 97%

Probing the binding of two 19‐nortestosterone derivatives to human serum albumin: insights into the interactions of steroid hormone drugs with functional biomacromolecule

Wang

et al. 2016

J of Molecular Recognition

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Norethindrone acetate (NETA) is a fatty acid ester of norethindrone (NET) that can convert to its more active parent compound NET when orally administered. To study the interactions of NETA and NET with human serum albumin (HSA), we applied fluorescence spectroscopy, circular dichroism (CD), and molecular docking. The effects of metal ions on the HSA-NETA/NET system were also explored. Fluorescence data showed that the quenching mechanism of HSA by NETA and NET was consistent with a static model and that the binding constant of NETA was higher than that of NET. Thermodynamic parameters indicated that hydrogen bonds and van der Waals forces were the main forces maintaining the stability of the HSA-NETA/NET complex. Molecular modeling studies revealed that NETA and NET were bound within subdomain IIA of HSA, in accordance with the site probe results. Synchronous fluorescence spectroscopy, CD, and three-dimensional fluorescence spectroscopy further confirmed that the binding of NETA/NET to HSA changed the secondary structure of the protein. All other metal ions, except for Ca(2+) , decreased the K value of the HSA-NETA/NET system with enhancement of the maximum effectiveness of NETA/NET. Three commercially available steroid hormone drugs influenced the binding ability of NETA on HSA to different extents. This study provides novel insights into the interactions between HSA and NETA/NET, as well as a solid foundation for future research on drug pharmacokinetics and pharmacodynamics. Copyright © 2016 John Wiley & Sons, Ltd.

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“…The biological activity of HSA will be changed due to the structure variation of it [40]; therefore La NPs can change the biological activity of HSA significantly. 3.9 3D fluorescence spectroscopy 3D fluorescence spectroscopy is used to probe the conformational changes in structure of proteins [41][42][43]. We obtained the 3D spectra of HSA and HSA-La NPs system (Fig.…”

Section: Discussionmentioning

confidence: 99%

Probing the in vitro binding mechanism between human serum albumin and La ₂ O ₂ CO ₃ nanoparticles

Shahraki¹,

Saeidifar²,

Gomroki³

2018

IET nanobiotechnol.

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The interaction of La 2 O 2 CO 3 nanoparticles (La NPs) with human serum albumin (HSA) has been studied. Analysis of the fluorescence quenching data of HSA using Stern-Volmer method showed that La NPs quenched HSA fluorescence in static quenching mode. Thermodynamic analysis indicated that hydrogen bonds and Van der Waals interactions play a major role for HSA-La NPs associations. Fluorescent displacement measurements confirmed that the primary binding site of La NPs was mainly located within site I (subdomain IIA) of HSA. The binding distance was calculated by using Forster resonance energy transfer theory. Also, the results of Fourier-transform infrared spectroscopy, circular dichroism, three-dimensional fluorescence and UV-visible measurements indicated that the binding of above La NPs to HSA may induce conformational and microenvironmental changes of protein. This study suggested that the conformational change of HSA was at secondary structure of it and the biological activity of this protein was changed in the present of La NPs.

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Probing the binding interaction of human serum albumin with three bioactive constituents of Eriobotrta japonica leaves: Spectroscopic and molecular modeling approaches

Cited by 18 publications

References 35 publications

Corosolic acid, a natural triterpenoid, induces ER stress-dependent apoptosis in human castration resistant prostate cancer cells via activation of IRE-1/JNK, PERK/CHOP and TRIB3

Corosolic acid, a natural triterpenoid, induces ER stress-dependent apoptosis in human castration resistant prostate cancer cells via activation of IRE-1/JNK, PERK/CHOP and TRIB3

Probing the binding of two 19‐nortestosterone derivatives to human serum albumin: insights into the interactions of steroid hormone drugs with functional biomacromolecule

Probing the in vitro binding mechanism between human serum albumin and La ₂ O ₂ CO ₃ nanoparticles

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Probing the binding interaction of human serum albumin with three bioactive constituents of Eriobotrta japonica leaves: Spectroscopic and molecular modeling approaches

Cited by 18 publications

References 35 publications

Corosolic acid, a natural triterpenoid, induces ER stress-dependent apoptosis in human castration resistant prostate cancer cells via activation of IRE-1/JNK, PERK/CHOP and TRIB3

Corosolic acid, a natural triterpenoid, induces ER stress-dependent apoptosis in human castration resistant prostate cancer cells via activation of IRE-1/JNK, PERK/CHOP and TRIB3

Probing the binding of two 19‐nortestosterone derivatives to human serum albumin: insights into the interactions of steroid hormone drugs with functional biomacromolecule

Probing the in vitro binding mechanism between human serum albumin and La 2 O 2 CO 3 nanoparticles

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Probing the in vitro binding mechanism between human serum albumin and La ₂ O ₂ CO ₃ nanoparticles