Probing the binding sites and the effect of berbamine on the structure of bovine serum albumin

Cheng, Xiaohuan; Lui, Y.; Zhou, Bo; Xiao, Xiaohe; Liu, Yi

doi:10.1016/j.saa.2008.12.003

Cited by 97 publications

(30 citation statements)

References 26 publications

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“…[45,47] Ranging from 0 (perpendicular dipole) to 4 (parallel dipole), generally the dipoles are assumed to be rapidly moving on a timescale similar to the donor excited-state lifetime. Their orientation is, therefore, described as random, with K 2 = 2/3.…”

Section: Fluorescence Resonance Energy Transfermentioning

confidence: 99%

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Interaction of Globular Plasma Proteins with Water‐Soluble CdSe Quantum Dots

et al. 2015

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The interactions between water-soluble semiconductor quantum dots [hydrophilic 3-mercaptopropionic acid (MPA)-coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β-lactoglobulin (β-Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecules form electrostatic interactions with these quantum dots (QDs). To determine the stoichiometry of proteins bound to QDs, we used dynamic light scattering (DLS) and zeta potential techniques. Fluorescence resonance energy transfer (FRET) experiments revealed energy transfer from tryptophan residues in the proteins to the QD particles. Quenching of the intrinsic fluorescence of protein molecules was noticed during this binding process (hierarchy HSA<β-Lg

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Section: Fluorescence Resonance Energy Transfermentioning

confidence: 99%

“…[46] The CD result was expressed in terms of mean residue ellipticity (MRE) in deg cm 2 dmol À1 [Eq. (14)]: [47] MRE ¼ ½qðm degÞ…”

Section: Effects On Secondary Structurementioning

confidence: 99%

Interaction of Globular Plasma Proteins with Water‐Soluble CdSe Quantum Dots

et al. 2015

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“…These values suggest that the energy transfer from BSA to NSTT occurs with high probability, because r is much \ 7 nm. So, the static quenching mechanism caused by binding of NSTT with BSA is responsible for fluorescence quenching [33,34].…”

Section: Energy Transfer Between Bsa and Nsttmentioning

confidence: 99%

Investigation of the Interaction Between Novel Spiro Thiazolo[3,2-a][1,3,5]Triazines and Bovine Serum Albumin by Spectroscopic Methods

Yang

Tong

et al. 2013

J Solution Chem

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The interaction between novel spiro thiazolo[3,2-a][1,3,5]triazines (NSTT) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy at different temperatures (302 and 310 K) under imitated physiological conditions. The experimental results show that the fluorescence quenching mechanism between NSTT and BSA is by a static quenching mechanism. The binding constant (K a ) and number of binding sites (n) between NSTT and BSA at different temperatures were obtained. Negative values of DG°, DH°, and DS°indicate that the interaction between NSTT and BSA is driven by hydrogen bonds and van der Waals forces. Using the Förster nonradiation energy transfer theory, the binding distance between BSA and NSTT was calculated. These results provide valuable information on the interaction between NSTT and BSA as well as the influence of substituent groups on the interaction.

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“…The most popularly studied albumins are bovine serum albumin (BSA) and human serum albumin (HSA). BSA and HSA display approximately 80% sequence homology [9,10]. BSA has two tryptophan residues that possess intrinsic fluorescence [11].…”

Section: Introductionmentioning

confidence: 99%