Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

Cheng, Li-Yang; Fang, Min; Bai, Ai‐Min; Ouyang, Yu; Hu, Yanjun

doi:10.1002/bio.3267

Cited by 15 publications

(5 citation statements)

References 47 publications

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“…The full fluorescence quenching of MTX was observed at very low concentrations (less than 0.5 mg/mL), demonstrating the strong binding of MTX with plasma protein, as reported previously [78]. Taking into account the strong interaction of MTX and almost inert behavior of LDH, the fluorescence quenching of MTX-LDH could be interpreted as the action of surface-adsorbed MTX on LDH particles [79,80]. To determine the type of quenching occurring in MTX-LDH, the experimental data were fitted to several models, including the Stern-Volmer, Perrin, and polynomial equations [81], as shown in Figure S6 and Table 1.…”

Section: Fluorescence Quenchingsupporting

confidence: 77%

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Blood Compatibility of Drug–Inorganic Hybrid in Human Blood: Red Blood Cell Hitchhiking and Soft Protein Corona

Xie,

Kim,

Kamada

et al. 2023

Materials

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A drug-delivery system consisting of an inorganic host—layered double hydroxide (LDH)—and an anticancer drug—methotrexate (MTX)—was prepared via the intercalation route (MTX-LDH), and its hematocompatibility was investigated. Hemolysis, a red blood cell counting assay, and optical microscopy revealed that the MTX-LDH had no harmful toxic effect on blood cells. Both scanning electron microscopy and atomic force microscopy exhibited that the MTX-LDH particles softly landed on the concave part inred blood cells without serious morphological changes of the cells. The time-dependent change in the surface charge and hydrodynamic radius of MTX-LDH in the plasma condition demonstrated that the proteins can be gently adsorbed on the MTX-LDH particles, possibly through protein corona, giving rise to good colloidal stability. The fluorescence quenching assay was carried out to monitor the interaction between MTX-LDH and plasma protein, and the result showed that the MTX-LDH had less dynamic interaction with protein compared with MTX alone, due to the capsule moiety of the LDH host. It was verified by a quartz crystal microbalance assay that the surface interaction between MTX-LDH and protein was reversible and reproducible, and the type of protein corona was a soft one, having flexibility toward the biological environment.

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Section: Fluorescence Quenchingsupporting

confidence: 77%

“…16, 6523 11 of 17MTX and almost inert behavior of LDH, the fluorescence quenching of MTX-LDH could be interpreted as the action of surface-adsorbed MTX on LDH particles[79,80].…”

mentioning

confidence: 99%

Blood Compatibility of Drug–Inorganic Hybrid in Human Blood: Red Blood Cell Hitchhiking and Soft Protein Corona

Xie,

Kim,

Kamada

et al. 2023

Materials

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“…Hydrophobic interactions also contributed to the binding between BSA and MTX, evidenced by the entropically favorable isotherms (ΔS ∼ 18 cal/mol °C at 25 °C and ionic strength of 15 mM). 63 Collectively, we determined electrostatic attractions as the main determinant to the binding between BSA and MTX, which can be modulated by changing the ionic strength of the solution.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Stimulus-Responsive Nanoconjugates Derived from Phytoglycogen Nanoparticles

Adibnia

Mitrache

et al. 2022

Biomacromolecules

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Plant-derived phytoglycogen nanoparticles (PhG NPs) have the advantages of size uniformity, dispersibility in water, excellent lubrication properties, and lack of cytotoxicity; however, their chemical functionalization may lead to loss of NP structural integrity. Here, we report a straightforward approach to the generation of PhG NP conjugates with biologically active molecules. Hydrogen bonding of bovine serum albumin with electroneutral PhG NPs endows them with additional ligand binding affinity and enables the electrostatically governed attachment of methotrexate (MTX), a therapeutic agent commonly used in the treatment of cancer and arthritis diseases, to the protein-capped NPs. We showed stimuli-responsive release of MTX from the PhG-based nanoconjugates under physiological cues such as temperature and ionic strength. The results of this study stimulate future exploration of biomedical applications of nanoconjugates of PhG NPs.

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“…SFS reflects information about the micro‐environment in the neighborhood of the fluorophore groups . The change of polarity around the Trp residue micro‐environment was obtained by setting the excitation and emission wavelength interval (Δλ) to 60 nm.…”

Section: Resultsmentioning

confidence: 99%

Probing the interaction of cephalosporin with bovine serum albumin: A structural and comparative perspective

Cheng

Yang

et al. 2017

Luminescence

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Cephalosporins belong the largest class of antibiotics used in the treatment of a wide range of infectious diseases caused by susceptible organisms. In the present study, we chose two typical antibiotics cefalexin/cefixime based on their structure, and investigated the interaction of cephalexin/cefixime with bovine serum albumin (BSA) using UV-vis absorption spectra, fluorescence spectroscopy, circular dichroism (CD) spectroscopy and molecular modeling approaches. Spectroscopic experiments revealed the formation of a BSA − cefalexin/cefixime complex. The binding parameters calculated using a modified Stern − Volmer method and the Scatchard method reached 10 3 -10 4 L·mol −1 . Thermodynamic parameter studies revealed that binding characteristics by negative enthalpy and positive entropy changes, and electrostatic interactions play a major role. Site marker competitive displacement experiments and molecular modeling approaches demonstrated that cefalexin and cefixime bind with appropriate affinity to site I (subdomain IIA) of BSA. Furthermore, synchronous fluorescence spectra, CD spectra and molecular modeling results indicated that the secondary structure of BSA was changed in the presence of cefalexin and cefixime. Additionally, the effects of metal ions on the BSA − cefalexin/cefixime system were also assessed.

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Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

Cited by 15 publications

References 47 publications

Blood Compatibility of Drug–Inorganic Hybrid in Human Blood: Red Blood Cell Hitchhiking and Soft Protein Corona

Blood Compatibility of Drug–Inorganic Hybrid in Human Blood: Red Blood Cell Hitchhiking and Soft Protein Corona

Stimulus-Responsive Nanoconjugates Derived from Phytoglycogen Nanoparticles

Probing the interaction of cephalosporin with bovine serum albumin: A structural and comparative perspective

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