Tracking structural transitions of bovine serum albumin in surfactant solutions by fluorescence correlation spectroscopy and fluorescence lifetime analysis

Soft Matter ◽  
2015 ◽  
Vol 11 (12) ◽  
pp. 2512-2518 ◽  
Author(s):  
Xuzhu Zhang ◽  
Andrzej Poniewierski ◽  
Sen Hou ◽  
Krzysztof Sozański ◽  
Agnieszka Wisniewska ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Lifetime ◽  
Fluorescence Correlation Spectroscopy ◽  
Bovine Serum ◽  
Structural Changes ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation ◽  
Surfactant Solutions ◽  
Lifetime Analysis

Sudden structural changes of BSA in surfactant solutions are observed from FCS curves.

Hydrogen—Deuterium Exchange in Bovine Serum Albumin Protein Monitored by Fourier Transform Infrared Spectroscopy, Part I: Structural Studies

2005 ◽  
Vol 59 (11) ◽  
pp. 1347-1356 ◽  
Author(s):  
Jože Grdadolnik ◽  
Yves Maréchal
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Structural Changes ◽  
Helical Structure ◽  
Correlation Spectroscopy ◽  
Side Chains ◽  
Hydrogen Atoms ◽  
Oh Groups ◽  
Higher Temperature

The structure of the amide I band of bovine serum albumin (BSA) was determined using an H/D exchange experiment. The difference between the dry and hydrated exchange spectrum revealed the fine structure of the amide I band. The band at 1717 ± 2 cm−1 is due to the vibration of the COOH moieties from the protein side chains. Band components at 1682 ± 2 cm−1, 1655 ± 2 cm−1, and 1637 ± 2 cm−1 are assigned to the vibrations of the backbone C=O. These three bands belong to vibrations of three different populations of amide groups differing in the number of established H-bonds. The connectivity between the frequencies of various amide vibrations was determined by two-dimensional generalized correlation spectroscopy and spectral decomposition. About 7% of the whole exchangeable hydrogen atom population (NH, NH2, and OH groups from backbone and side chains) remains unexchanged, and these hydrogen atoms belong mainly to the NH groups, which are H-bonded to specific C=O groups. Moreover, this study concerns the approximately 10% of hydrogen atoms belonging to a particular HN … OC population with a characteristic amide A frequency at 3290 cm−1 and an amide I band at 1655 ± 2 cm−1, usually attributed to the α-helical structure that remains unexchanged. At higher temperature the exchange is more efficient. Upon heating, a further 4% of these NH groups are deuterated. The comparison of the exchange spectrum at higher temperature with the structural changes of the protein at the same temperature implies that the change in overall dynamics of the protein improve the level of exchange.

scholarly journals The application of two-dimensional fluorescence correlation spectroscopy on the interaction between bovine serum albumin and prulifloxacin

2009 ◽  
Vol 23 (5-6) ◽  
pp. 257-263 ◽  
Author(s):  
Mao-Yun Xue ◽  
Ai-Ping Yang ◽  
Mei-Hua Ma ◽  
Xiao-Hua Li
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Resolution Enhancement ◽  
Correlation Spectroscopy ◽  
Two Dimensional ◽  
Fluorescence Correlation ◽  
Enthalpy Changes ◽  
2D Correlation Spectroscopy

The interaction between bovine serum albumin (BSA) and prulifloxacin was investigated by ultraviolet spectrophotometer (UV) and fluorescence spectroscopy in this paper. Two-dimensional (2D) correlation spectroscopy was applied to the analysis of fluorescence spectra. The results of spectroscopic measurements suggested that prulifloxacin (PL) have a strong ability to quench the intrinsic fluorescence of bovine serum albumin through static quenching procedure. Thermodynamic parameter enthalpy changes (ΔH) and entropy changes (ΔS) were calculated. Owing to the spectral resolution enhancement in 2D correlation spectroscopy, the structure change of prulifloxacin can be observed.

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