Spectroscopic and biophysical approaches for studying the structure and function of the P-glycoprotein multidrug transporter

1998 ◽  
Vol 76 (5) ◽  
pp. 695-708 ◽  
Author(s):  
Frances J Sharom ◽  
Ronghua Liu ◽  
Yolanda Romsicki
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Multidrug Resistance ◽  
Fluorescence Spectroscopy ◽  
Lipid Bilayers ◽  
Drug Transport ◽  
Circular Dichroism Spectroscopy ◽  
P Glycoprotein ◽  
Infra Red ◽  
Circular Dichroïsm

Multidrug resistance is a serious obstacle to the successful chemotherapeutic treatment of many human cancers. A major cause of multidrug resistance is the overexpression of a 170-kDa plasma membrane protein, known as P-glycoprotein, which appears to function as an ATP-driven efflux pump with a very broad specificity for hydrophobic drugs, peptides, and natural products. P-Glycoprotein is a member of the ABC superfamily and is proposed to consist of two homologous halves, each comprising six membrane-spanning segments and a cytosolic nucleotide binding domain. In recent years, P-glycoprotein has been purified and functionally reconstituted into lipid bilayers, where it retains both ATPase and drug transport activity. The availability of purified active protein has led to substantial advances in our understanding of the molecular structure and mechanism of action of this unique transporter. This review will focus on the recent application of fluorescence spectroscopy, infra-red spectroscopy, circular dichroism spectroscopy, electron microscopy, and other biophysical techniques to the study of P-glycoprotein structure and function.Key words: multidrug resistance, P-glycoprotein, fluorescence spectroscopy, infra-red spectroscopy, circular dichroism spectroscopy, differential scanning calorimetry, electron microscopy.

Insights into the binding of photothermal therapeutic agent bismuth sulfide nanorods with human serum albumin

RSC Advances ◽  
2016 ◽  
Vol 6 (20) ◽  
pp. 16215-16222 ◽  
Author(s):  
Selvaraj Naveenraj ◽  
Ramalinga Viswanathan Mangalaraja ◽  
Jerry J. Wu ◽  
Abdullah M. Asiri ◽  
Sambandam Anandan
Keyword(s):  
Circular Dichroism ◽  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Absorption Spectroscopy ◽  
Therapeutic Agent ◽  
Circular Dichroism Spectroscopy ◽  
Bismuth Sulfide ◽  
Circular Dichroïsm

The interaction of microwave synthesized bismuth sulfide nanorods with human serum albumin was investigated using multispectroscopic techniques such as absorption spectroscopy, fluorescence spectroscopy and circular dichroism spectroscopy.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

scholarly journals Conformation Transition Kinetics of Silk Fibroin in Aqueous Solution Explored Using Circular Dichroism Spectroscopy

2021 ◽  
Vol 6 (8) ◽  
pp. 1735-1740
Author(s):  
Sora Lee ◽  
Soo Hyun Kim ◽  
You‐Young Jo ◽  
Wan‐Taek Ju ◽  
Hyun‐Bok Kim ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Circular Dichroism ◽  
Silk Fibroin ◽  
Circular Dichroism Spectroscopy ◽  
Kinetics Of ◽  
Circular Dichroïsm ◽  
Conformation Transition

Enantiopure methoxetamine stereoisomers: chiral resolution, conformational analysis, UV-circular dichroism spectroscopy and electronic circular dichroism

2021 ◽  
Author(s):  
Kun Won Lee ◽  
Ahmed H. E. Hassan ◽  
Youngdo Jeong ◽  
Seolmin Yoon ◽  
Seung-Hwan Kim ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Conformational Analysis ◽  
Absolute Configuration ◽  
Circular Dichroism Spectroscopy ◽  
Chiral Resolution ◽  
Treatment Resistant Depression ◽  
Treatment Resistant ◽  
Electronic Circular Dichroism ◽  
Resistant Depression ◽  
Circular Dichroïsm

Enantioseparation and assignment of absolute configuration of methoxetamine (MXE) enantiopure stereoisomers; a promising novel antidepressant for management of treatment-resistant depression.

scholarly journals Circular dichroism spectroscopy of membrane proteins

2016 ◽  
Vol 45 (18) ◽  
pp. 4859-4872 ◽  
Author(s):  
A. J. Miles ◽  
B. A. Wallace
Keyword(s):  
Circular Dichroism ◽  
Membrane Proteins ◽  
Circular Dichroism Spectroscopy ◽  
Circular Dichroism Spectra ◽  
Helical Bundle ◽  
Beta Barrel ◽  
Circular Dichroïsm

Circular dichroism spectra of helical bundle (red), beta barrel (blue), and mixed helical/sheet/unordered (green) membrane proteins.

scholarly journals Detection of Protein-Protein Interactions in the Alkanesulfonate Monooxygenase System from Escherichia coli

2006 ◽  
Vol 188 (23) ◽  
pp. 8153-8159 ◽  
Author(s):  
Kholis Abdurachim ◽  
Holly R. Ellis
Keyword(s):  
Circular Dichroism ◽  
Protein Interactions ◽  
Visible Region ◽  
Circular Dichroism Spectroscopy ◽  
Flavin Mononucleotide ◽  
Stable Complex ◽  
Monooxygenase System ◽  
Protein Protein Interactions ◽  
Alkanesulfonate Monooxygenase ◽  
Circular Dichroïsm

ABSTRACT The two-component alkanesulfonate monooxygenase system utilizes reduced flavin as a substrate to catalyze a unique desulfonation reaction during times of sulfur starvation. The importance of protein-protein interactions in the mechanism of flavin transfer was analyzed in these studies. The results from affinity chromatography and cross-linking experiments support the formation of a stable complex between the flavin mononucleotide (FMN) reductase (SsuE) and monooxygenase (SsuD). Interactions between the two proteins do not lead to overall conformational changes in protein structure, as indicated by the results from circular dichroism spectroscopy in the far-UV region. However, subtle changes in the flavin environment of FMN-bound SsuE that occur in the presence of SsuD were identified by circular dichroism spectroscopy in the visible region. These data are supported by the results from fluorescent spectroscopy experiments, where a dissociation constant of 0.0022 ± 0.0010 μM was obtained for the binding of SsuE to SsuD. Based on these studies, the stoichiometry for protein-protein interactions is proposed to involve a 1:1 monomeric association of SsuE with SsuD.

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