A spectroscopic study on the interaction between p-nitrophenol and bovine serum albumin

Guo, Xingjia; Li, Xiaozhou; Jiang, Yuchun; Li, Yi; Wu, Qiong; Chang, H. C.; Diao, Xin; Sun, Ye; Pan, Xintong; Zhou, Nannan

doi:10.1016/j.jlumin.2014.01.036

Cited by 84 publications

(41 citation statements)

References 23 publications

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“…The concentration of P9-1 proteins for each run was fixed at 10 μM, the concentration of α-amino phosphonate derivatives, respectively 0, 2, 4, 6, 8, 10, 12, 14, 16 and 18 μM. The decrease in fluorescence intensity at the highest peak was analyzed according to the Stern-Volmer equation [46]:…”

Section: Interaction Studies Between Nnm and Tmv Cpmentioning

confidence: 99%

Analysis and application of the SRBSDV P9-1 octamer crystal structure for the target of α-amino phosphonate derivatives

Ding¹,

Li²,

Chen³

et al. 2018

Oncotarget

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Southern rice black-streaked dwarf virus (SRBSDV) P9-1 octameric protein accumulates viroplasms in SRBSDV-infected plant and insect cells, our previous studies found α-amino phosphonate drug-dufulin had a micromole affinity with SRBSDV P9-1. Now we focus our studies on the SRBSDV P9-1 crystal structure and use it as the target for α-amino phosphonate derivatives. The structure of the SRBSDV P9-1 cylindrical octamer was determined to a 2.2 Å resolution using X-ray crystallography, this structure was composed of nine α-helices, nine β-sheets and a series of interconnecting loops. The structures of all eight subunits were nearly identical, except for some differences in the β-sheet core. There were six different sites (R20K, V109D, F164T, V123L, C124L and V128T) present between the SRBSDV P9-1 and the previously reported RBSDV P9-1 crystal structure. Fluorescence titration, isothermal calorimetry and microscale thermophoresis experiments showed that α-amino phosphonate derivatives GUFCC-013 and GUFCC-023 bound to SRBSDV P9-1 with micromole binding affinities. These results will provide important help for the further improvement of the lead compound and develop the potential anti-SRBSDV drugs.

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Section: Interaction Studies Between Nnm and Tmv Cpmentioning

confidence: 99%

Analysis and application of the SRBSDV P9-1 octamer crystal structure for the target of α-amino phosphonate derivatives

Ding¹,

Li²,

Chen³

et al. 2018

Oncotarget

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“…However, the intrinsic fluorescence of BSA mainly originate from Trp and Tyr residues when excited at 280 nm [14].…”

Section: Fluorescence Quenching Mechanism Of Bsa By Rlncsmentioning

confidence: 99%

“…Moreover, curve j was the fluorescence spectrum of RLNCs solution alone when excited at 280 nm, which demonstrated that Fluorescence quenching is the decrease of fluorescence intensity from a fluorophore induced by a variety of molecular interactions with quencher molecules. When pH, temperature and ionic strength are kept unchanged, fluorescence quenching may result from ground complex formation, energy transfer and dynamic quenching processes [14]. Dynamic quenching refers to any process that occurs during the excited-state lifetime of fluorophore, whereas static quenching refers to complex formation between fluorophore and quencher.…”

Section: Fluorescence Quenching Mechanism Of Bsa By Rlncsmentioning

confidence: 99%

“…Static quenching and dynamic quenching can be distinguished by their different dependence on temperature and excited-state lifetime [14]. Dynamic quenching depends upon diffusion: higher temperatures result in larger diffusion coefficients, in other word, quenching constants will increase with temperature rising.…”

Section: Fluorescence Quenching Mechanism Of Bsa By Rlncsmentioning

confidence: 99%

“…It consists of three linearly arranged domains (I-III), and each domain composed of two sub-domains (A, B). The principal regions of binding sites of albumin are located in hydrophobic cavities in sub-domains IIA and IIIA, namely so-called sites I and II [14]. Many ligands bind specifically to serum albumin, for example, phenylbutazone in site I [15], ibuprofen in site II [16].…”

Section: Introductionmentioning

confidence: 99%

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Binding nature and conformational alternations of bovine serum albumin upon interaction with synthesized LaF3:Ce,Tb luminescent nanocrystals using multi-spectroscopic approach

Guo

Hao

et al. 2016

Journal of Luminescence

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Aminobenzimidazole‐based (η⁶‐p‐cymene)ruthenium (II) complexes as nascent anticancer chemotherapeutics: Synthesis, crystal structure, DFT studies, HSA interactions, molecular docking, and cytotoxicity

Khan

AlFawaz

Farshori

et al. 2022

Applied Organom Chemis

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Two half‐sandwich organometallic ruthenium (II) complexes containing analogs of aminobenzimidazole of molecular formula [η6‐p‐cymene)Ru (LH)Cl2] 1 and [η6‐p‐cymene)Ru (LMe)Cl2] 2, where LH and LMe represent 2‐aminobenzimidazole and 2‐amino‐1‐methylbenzimidazole, respectively, have been synthesized and characterized by FT‐IR, NMR (1H, 13C), ESI‐MS, elemental analysis, and single X‐ray crystallography (for 1). Both complexes 1 and 2 were studied for human serum albumin (HSA) binding affinity using intrinsic, synchronous, three‐dimensional (3D) fluorescence, thermodynamics parameter, and Förster resonance energy transfer (FRET) analysis. The Stern–Volmer constant (KSV) values are of the order of ×105 M−1 and increases in KSV with temperature ascertained the static quenching. The molecular docking of both the complexes with HSA was carried out to ascertain the binding sites/pockets. Furthermore, compounds were evaluated for their cytotoxic potential against three human cancer cell lines, namely, HeLa, HepG2, MCF‐7, and non‐tumorigenic HEK293 cells. The IC50 value of 2 was found to <10 μM against Hela and HepG2 cancer cells and has better cytotoxic properties than cisplatin (a standard drug), yet showed minimal toxicity against HEK293 cells. These results suggest further investigation for the development of ruthenium complex 2 as potential anticancer therapeutics.

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A spectroscopic study on the interaction between p-nitrophenol and bovine serum albumin

Cited by 84 publications

References 23 publications

Analysis and application of the SRBSDV P9-1 octamer crystal structure for the target of α-amino phosphonate derivatives

Analysis and application of the SRBSDV P9-1 octamer crystal structure for the target of α-amino phosphonate derivatives

Binding nature and conformational alternations of bovine serum albumin upon interaction with synthesized LaF3:Ce,Tb luminescent nanocrystals using multi-spectroscopic approach

Aminobenzimidazole‐based (η⁶‐p‐cymene)ruthenium (II) complexes as nascent anticancer chemotherapeutics: Synthesis, crystal structure, DFT studies, HSA interactions, molecular docking, and cytotoxicity

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A spectroscopic study on the interaction between p-nitrophenol and bovine serum albumin

Cited by 84 publications

References 23 publications

Analysis and application of the SRBSDV P9-1 octamer crystal structure for the target of α-amino phosphonate derivatives

Analysis and application of the SRBSDV P9-1 octamer crystal structure for the target of α-amino phosphonate derivatives

Binding nature and conformational alternations of bovine serum albumin upon interaction with synthesized LaF3:Ce,Tb luminescent nanocrystals using multi-spectroscopic approach

Aminobenzimidazole‐based (η6‐p‐cymene)ruthenium (II) complexes as nascent anticancer chemotherapeutics: Synthesis, crystal structure, DFT studies, HSA interactions, molecular docking, and cytotoxicity

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Aminobenzimidazole‐based (η⁶‐p‐cymene)ruthenium (II) complexes as nascent anticancer chemotherapeutics: Synthesis, crystal structure, DFT studies, HSA interactions, molecular docking, and cytotoxicity