Optical and structural properties of plasma-treatedCordyceps bassianaspores as studied by circular dichroism, absorption, and fluorescence spectroscopy

2015 ◽  
Vol 117 (2) ◽  
pp. 023303 ◽  
Author(s):  
Geon Joon Lee ◽  
Geon Bo Sim ◽  
Eun Ha Choi ◽  
Young-Wan Kwon ◽  
Jun Young Kim ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Fluorescence Spectroscopy ◽  
Structural Properties ◽  
Absorption And Fluorescence Spectroscopy ◽  
Circular Dichroïsm

scholarly journals A Raman, SERS and UV-circular dichroism spectroscopic study of N-acetyl-l-cysteine in aqueous solutions

2019 ◽  
Vol 43 (38) ◽  
pp. 15201-15212 ◽  
Author(s):  
R. A. Cobos Picot ◽  
M. Puiatti ◽  
A. Ben Altabef ◽  
R. J. G. Rubira ◽  
S. Sanchez-Cortes ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Circular Dichroism ◽  
Aqueous Solutions ◽  
Spectroscopic Study ◽  
Electronic Properties ◽  
Structural Properties ◽  
Amine Groups ◽  
Circular Dichroïsm

The aim of this work is to evaluate the vibrational and structural properties of N-acetyl-l-cysteine (NAC), and its molecular structure and electronic properties in relation to the action of thiol and amine groups at different pH.

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.

scholarly journals Biological Activities and Structural Properties of the Atypical Bacteriocins Mesenterocin 52B and Leucocin B-TA33a

2001 ◽  
Vol 67 (4) ◽  
pp. 1418-1422 ◽  
Author(s):  
C. Corbier ◽  
F. Krier ◽  
G. Mulliert ◽  
B. Vitoux ◽  
A.-M. Revol-Junelles
Keyword(s):  
Circular Dichroism ◽  
Structural Properties ◽  
Sequence Homology ◽  
Synthetic Peptides ◽  
Biological Activities ◽  
Modes Of Action ◽  
Amphiphilic Helix ◽  
High Sequence Homology ◽  
Circular Dichroïsm

ABSTRACT The antibacterial spectra and modes of action of synthetic peptides corresponding to mesenterocin 52B and leucocin B-TA33a greatly differ despite their high sequence homology. Circular dichroism experiments establish the capacity of each of these two peptides to partly fold into an amphiphilic helix that might be crucial for their adsorption at lipophilic-hydrophilic interfaces.

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