Studies on the interaction between scopoletin and two serum albumins by spectroscopic methods

Cheng, Zhengjun

doi:10.1016/j.jlumin.2012.05.032

Cited by 82 publications

(40 citation statements)

References 42 publications

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“…The value of the binding constant of the α-tocopherol-bovine serum albumin (BSA) system obtained by ITC is 6.906 × 10 5 l mol −1 [6], and the binding constant is 4.142 × 10 3 l mol −1 for the α-tocopherol-human serum albumin (HSA) system obtained from spectroscopic methods [7]. They are moderate compared to other strong protein-ligand complexes with binding constants ranging from 10 7 -10 8 l mol −1 [27]. The value of the stoichiometric binding number approximately equals 1, suggesting that one molecule of α-tocopherol combines with one molecule of trypsin/pepsin and no more α-tocopherol binding to trypsin/pepsin occurs at concentration ranges used in this study.…”

Section: Isothermal Titration Calorimetry (Itc) Studiesmentioning

confidence: 99%

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

2016

J Biol Phys

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α-Tocopherol is a required nutrient for a variety of biological functions. In this study, the binding of α-tocopherol to trypsin and pepsin was investigated using isothermal titration calorimetry (ITC), steady-state and time-resolved fluorescence measurements, circular dichroism (CD) spectroscopy, and molecular modeling methods. Thermodynamic investigations reveal that α-tocopherol binds to trypsin/pepsin is synergistically driven by enthalpy and entropy. The fluorescence experimental results indicate that α-tocopherol can quench the fluorescence of trypsin/pepsin through a static quenching mechanism. The binding ability of α-tocopherol with trypsin/pepsin is in the intermediate range, and one molecule of α-tocopherol combines with one molecule of trypsin/pepsin. As shown by circular dichroism (CD) spectroscopy, α-tocopherol may induce conformational changes of trypsin/pepsin. Molecular modeling displays the specific binding site and gives information about binding forces and α-tocopherol-tryptophan (Trp)/tyrosine (Tyr) distances. In addition, the inhibition rate of α-tocopherol on trypsin and pepsin was studied. The study provides a basic data set for clarifying the binding mechanisms of α-tocopherol with trypsin and pepsin and is helpful for understanding its biological activity in vivo.

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Section: Isothermal Titration Calorimetry (Itc) Studiesmentioning

confidence: 99%

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

2016

J Biol Phys

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“…The relatively high cross-reactivity of the ferritin-imprinted MIP towards BSA is probably caused by the fact that the BSA molecule can interact via its tryptophan residues with the scopoletin moieties of the MIP layer. Such interaction was shown to occur between scopoletin as a drug molecule and serum albumins resulting in the formation of scopoletin-BSA complexes (Cheng, 2012). It is likely that the interaction persists also for polyscopoletin as an inherent property of the polymer film.…”

Section: Cross-reactivity Of the Protein-imprinted Spotsmentioning

confidence: 99%

Microelectrospotting as a new method for electrosynthesis of surface-imprinted polymer microarrays for protein recognition

Bosserdt

Erdőssy²,

Lautner

et al. 2015

Biosensors and Bioelectronics

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Here we introduce microelectrospotting as a new approach for preparation of protein-selective molecularly imprinted polymer microarrays on bare gold SPR imaging chips. During electrospotting both the gold chip and the spotting tip are electrically connected to a potentiostat as working and counter electrodes, respectively. The spotting pin encloses the monomer-template protein cocktail that upon contacting the gold surface is in-situ electropolymerized resulting in surface confined polymer spots of ca. 500 µm diameter. By repeating this procedure at preprogrammed locations for various composition monomer-template mixtures microarrays of nanometer-thin surface-imprinted films are generated in a controlled manner. We show that the removal and rebinding kinetics of the template and various potential interferents to such microarrays can be monitored in real-time and multiplexed manner by SPR imaging. The proof of principle for microelectrospotting of electrically insulating surface-imprinted films is made by using scopoletin as monomer and ferritin as protein template. It is shown that microelectrospotting in combination with SPR imaging can offer a versatile platform for label-free and enhanced throughput optimization of the molecularly imprinted polymers for protein recognition and for their analytical application.

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“…The native conformation of HSA has two principal hydrophobic binding sites, called sites I and II (Sudlow, Birkett, & Wade, 1975), located in subdomains IIA and IIIA (He & Carter, 1992) and it is generally assumed that in BSA and HSA these sites are homologous. From the spectroscopic point of view, one of the main differences between the two proteins is that HSA has one tryptophan (Trp-214) in subdomain IIA, whereas BSA has two tryptophan moieties (Trp-134 and Trp-212) located in subdomains IB and IIA, respectively (Cheng, 2012). Trp-212 residue is surrounded by a hydrophobic environment within a protein pocket while Trp-134 residue is located in a hydrophilic environment, close to the protein surface (Peters, 1985).…”

Section: Introductionmentioning

confidence: 99%

β-Carotene and astaxanthin with human and bovine serum albumins

Wang

Chen

et al. 2015

Food Chemistry

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Studies on the interaction between scopoletin and two serum albumins by spectroscopic methods

Cited by 82 publications

References 42 publications

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

Microelectrospotting as a new method for electrosynthesis of surface-imprinted polymer microarrays for protein recognition

β-Carotene and astaxanthin with human and bovine serum albumins

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