Spectroscopic investigations on the binding of leucomalachite green to bovine serum album

Zeng, Xiaodan; Zhu, Lin; Zhang, FuSheng; Feng, Liyun

doi:10.1016/j.jlumin.2012.12.034

Cited by 5 publications

(2 citation statements)

References 26 publications

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“…The interaction of drugs with HSA increases drug solubility in vivo and significantly affects their metabolic rate . Thus, the study of the interaction between serum albumin and drugs remains a focus topic among scientists to better understand the biodistribution, metabolism, elimination, and pharmacological effects of drugs in the body .…”

Section: Introductionmentioning

confidence: 99%

Investigations on the interactions between naphthalimide‐based anti‐tumor drugs and human serum albumin by spectroscopic and molecular modeling methods

Cheng

Zou

et al. 2015

Luminescence

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The interactions between the three kinds of naphthalimide-based anti-tumor drugs (NADA, NADB, NADC) and human serum albumin (HSA) under simulated physiological conditions were investigated by fluorescence spectroscopy, circular dichroism spectroscopy and molecular modeling. The results of the fluorescence quenching spectroscopy showed that the quenching mechanisms for different drugs were static and their affinity was in a descending order of NADA > NADB > NADC. The relative thermodynamic parameters indicated that hydrophobic force was the predominant intermolecular force in the binding of NAD to HSA, while van der Waals interactions and hydrogen bonds could not be ignored. The results of site marker competitive experiment confirmed that the binding site of HSA primarily took place in site I. Furthermore, the molecular modeling study was consistent with these results. The study of circular dichroism spectra demonstrated that the presence of NADs decreased the α-helical content of HSA and induced the change of the secondary structure of HSA.

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Section: Introductionmentioning

confidence: 99%

Investigations on the interactions between naphthalimide‐based anti‐tumor drugs and human serum albumin by spectroscopic and molecular modeling methods

Cheng

Zou

et al. 2015

Luminescence

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“…The presence of tryptophan residues offers an advantage to studying the ligand binding process using fluorescence spectroscopy [14]. The interactions between drugs and protein can been studied by fluorescence spectroscopy [15][16][17][18][19]. Therefore, the association behaviors between the synthesized compounds (W 3 and W 4 ) and FTO were investigated by spectroflourimetric method for the first time.…”

Section: Introductionmentioning

confidence: 99%

Influence of the Ring Size on the Binding Ability of FTO Investigated by Fluorescence Spectroscopy

Yang

et al. 2015

J Fluoresc

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The fat mass and obesity associated protein (FTO) is a potential target for anti-obesity medicines. In this paper, we have synthesized two potential inhibitors for FTO, three-member-ring compound (W 3 ) and four-member-ring compound (W 4 ). The interactions of fat mass and obesity-associated (FTO) protein with W 3 (or W 4 ) have been studied by spectral method. Results show the intrinsic fluorescence is quenched by the W 3 (or W 4 ). The thermodynamics parameters indicate hydrophobic interaction play a major role in the interactions. The results of synchronous fluorescence spectra demonstrate that the microenvironments of Trp residue of FTO are disturbed by W 3 and W 4 . Results showed that W 3 are stronger quenchers and bind to FTO with the higher affinity than W 4 . The influence of molecular structure on the binding aspects has been investigated.

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Nitidine chloride-assisted bio-functionalization of reduced graphene oxide by bovine serum albumin for impedimetric immunosensing

Zhang

et al. 2016

Biosensors and Bioelectronics

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Spectroscopic investigations on the binding of leucomalachite green to bovine serum album

Cited by 5 publications

References 26 publications

Investigations on the interactions between naphthalimide‐based anti‐tumor drugs and human serum albumin by spectroscopic and molecular modeling methods

Investigations on the interactions between naphthalimide‐based anti‐tumor drugs and human serum albumin by spectroscopic and molecular modeling methods

Influence of the Ring Size on the Binding Ability of FTO Investigated by Fluorescence Spectroscopy

Nitidine chloride-assisted bio-functionalization of reduced graphene oxide by bovine serum albumin for impedimetric immunosensing

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