Enhancement of the binding affinity of methylene blue to site I in human serum albumin by cupric and ferric ions

He, Lihua; Wang, Yongxia; Wu, Xiaoxia; Liu, Xian-Ping; Wang, Xin; Liu, Bin

doi:10.1002/bio.2910

Cited by 14 publications

(5 citation statements)

References 64 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This led us to propose both that the concentration of free MB was very small in solution when BSA was at high concentrations and, also, that SOCL and MB had to form a ternary complex together with BSA. Co-operative binding of two ligands to BSA or HSA has been previously reported [27,38]. Further evidence for the ternary complex in our study was the subtracting effect of SOCL on the overall oxygen consumption rate when BSA was present in solution.…”

Section: Discussionsupporting

confidence: 84%

“…MB (or MB/TiO 2 ) is known to bind predominantly to BSA or HSA in one single site. MB binds to BSA or HSA within the sub-domain IIA with a moderate association constant, whose values range from 2.4 × 10 3 M −1 [36] to 7.6 × 10 4 M −1 [37] for BSA and from 4.0 × 10 4 M −1 [38] to 4.3 × 10 4 M −1 [39] for HSA. Based on the former association constants, the BSA-bound MB was calculated to increase by approximately 8–10% when the BSA concentration went from 45 μM to 90 μM in the reaction mixture.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Emissive Enhancement of the Singlet Oxygen Chemiluminescence Probe after Binding to Bovine Serum Albumin

et al. 2019

View full text Add to dashboard Cite

A chemiluminescence probe for singlet oxygen 1O2 (SOCL) was investigated in phosphate buffer saline (PBS), either in the absence of proteins or containing bovine serum albumin (BSA). In the protein-free PBS, the reactivity of SOCL for methylene blue (MB)-photosensitized 1O2 was found to be moderate or low. The reaction yield increased with temperature and/or concentration of dissolved molecular oxygen. Unexpectedly, the presence of BSA boosted both the emissive nature and the thermal stability of the phenoxy-dioxetane intermediate formed in the chemiexcitation pathway. Isothermal titration calorimetry showed that SOCL has a moderate binding affinity for BSA and that entropy forces drive the formation of the SOCL-BSA complex. A model with two identical and independent binding sites was used to fit the binding isotherm data. Co-operative binding was observed when MB was present. Local viscosity factors and/or conformational restrictions of the BSA-bound SOCL phenoxy-dioxetane were proposed to contribute to the formation of the highly emissive benzoate ester during the chemically initiated electron exchange luminescence (CIEEL) process. These results led us to conclude that hydrophobic interactions of the SOCL with proteins can modify the emissive nature of its phenoxy-dioxetane, which should be taken into account when using SOCL or its cell-penetrating peptide derivative in living cells.

show abstract

Section: Discussionsupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Emissive Enhancement of the Singlet Oxygen Chemiluminescence Probe after Binding to Bovine Serum Albumin

et al. 2019

View full text Add to dashboard Cite

show abstract

“…In this study, KP and IB are used as Site I‐ and Site II‐specific binding site markers. [ 49,50 ] By observing the change in the binding constants after adding CBZ to the probe–BSA system, we can determine the specific binding site of CBZ on BSA. Table 4 records the binding constants of the CBZ–BSA system before and after adding a competitive reagent.…”

Section: Resultsmentioning

confidence: 99%

The influence of several nutritional supplements on the rational use of cabozantinib

Duan

Wang²,

Liu

et al. 2022

Luminescence

Self Cite

View full text Add to dashboard Cite

To promote the rational use of cabozantinib (CBZ), this paper studied the influence of several nutritional supplements on the interaction between CBZ and bovine serum albumin (BSA), an appropriate alternative model for human serum albumin (HSA) that is one of the important transporter proteins in plasma, by fluorescence spectroscopy and UV–vis spectroscopy. The results showed that CBZ could quench the fluorescence of BSA via a dynamic–static quenching process, and the six nutritional supplements did not change the quenching mode of BSA by CBZ. However, all of them could reduce the binding constant of the CBZ–BSA system at 293 K and increase the polarity around tryptophan residues. Among them, nicotinamide and vitamin B12 (VB12) had a greater effect on the binding constants of the CBZ–BSA system. In the meantime, the thermodynamic parameters of the CBZ–BSA system were examined, indicating that the interaction of CBZ with BSA was spontaneous and dominated by hydrophobic forces. Further research discovered that the combining of CBZ with BSA was primarily located within Site I of BSA, and the binding distance r was 2.48 nm. Consequently, while taking CBZ, patients should use VB12 and nicotinamide carefully, which may interfere with the transport of drugs.

show abstract

“…Due to the high affinity of ICG/MB to HSA, the two dyes were simultaneously inserted into the subdomain of HSA matrix via highly hydrophobic interactions. 49 , 50 Molecular docking was performed using AutoDock Vina software in order to visually reveal the binding modes of ICG/MB within HSA. The simulation results indicate that ICG and MB could selectively bind to the subdomain IIA of HSA, and the distance of the two dyes is less than 2 nm (Figure 1 b).…”

Section: Resultsmentioning

confidence: 99%

Förster Resonance Energy Transfer-Based Dual-Modal Theranostic Nanoprobe for In Situ Visualization of Cancer Photothermal Therapy

Sheng

Zhu

et al. 2018

Theranostics

View full text Add to dashboard Cite

The visualization of the treatment process in situ could facilitate to accurately monitor cancer photothermal therapy (PTT), and dramatically decrease the risk of thermal damage to normal cells and tissues, which represents a major challenge for cancer precision therapy. Herein, we prepare theranostic nanoprobes (NPs) for Förster resonance energy transfer (FRET)-based dual-modal imaging-guided cancer PTT, and clear visualization of the therapeutic process. The FRET-based theranostic NPs exhibit high FRET efficiency (88.2%), good colloidal stability, and tumor-targeting ability. Tumor tissue and surrounding blood vessels are visualized clearly by FRET-based NIR fluorescence imaging with a high signal-to-background ratio (14.5) and photoacoustic imaging with an excellent resolution at 24 h post injection of NPs. Under the guidance of dual-modal imaging, the NPs-induced photothermal effect selectively destructs cancer cells, simultaneously decreasing the FRET efficiency and leading to fluorescence and photoacoustic signal changes. The sensitive self-feedback process enables the in situ visualization of therapeutic process and precision guidance of in vivo cancer PTT. A high therapeutic efficacy and minimum side effects are achieved in C6 tumor-bearing nude mice, holding great promise for precision therapy and cancer theranostics.

show abstract

Enhancement of the binding affinity of methylene blue to site I in human serum albumin by cupric and ferric ions

Cited by 14 publications

References 64 publications

Emissive Enhancement of the Singlet Oxygen Chemiluminescence Probe after Binding to Bovine Serum Albumin

Emissive Enhancement of the Singlet Oxygen Chemiluminescence Probe after Binding to Bovine Serum Albumin

The influence of several nutritional supplements on the rational use of cabozantinib

Förster Resonance Energy Transfer-Based Dual-Modal Theranostic Nanoprobe for In Situ Visualization of Cancer Photothermal Therapy

Contact Info

Product

Resources

About