Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin
Pterodontic acid (PA) has been isolated from Laggera pterodonta, a Chinese herbal medicine, and shown to possess antibacterial activity in vitro. To facilitate its preclinical development, the interaction between PA and bovine serum albumin (BSA) was studied using a fluorescence quenching technique,...
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2012-02-01
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doaj-cd3944b5d92c4d4ebdfa52d5f58024ff2020-11-24T22:48:05ZengElsevierActa Pharmaceutica Sinica B2211-38352211-38432012-02-0121535910.1016/j.apsb.2011.12.001Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albuminYunfang LiGuangzhong YangZhinan MeiPterodontic acid (PA) has been isolated from Laggera pterodonta, a Chinese herbal medicine, and shown to possess antibacterial activity in vitro. To facilitate its preclinical development, the interaction between PA and bovine serum albumin (BSA) was studied using a fluorescence quenching technique, ultraviolet–visible spectrophotometry and dynamic light scattering (DLS). At temperatures of 297 K and 310 K and an excitation wavelength of 282 nm, the fluorescence intensity of BSA decreased significantly with increasing concentration of PA attributed to the formation of a PA–BSA complex. The apparent binding constant, number of binding sites and corresponding thermodynamic parameters were calculated and the main intermolecular attraction shown to result from hydrogen bonding and van der Waals forces. Synchronous fluorescence spectrometry revealed that the binding site in the complex approached the microenvironment of Trp and three-dimensional fluorescence spectroscopy showed the binding induced conformational changes in BSA. Using DLS, increasing PA concentration was shown to cause a gradual increase in hydrodynamic diameter and significant aggregation of the complex.http://www.sciencedirect.com/science/article/pii/S2211383511001031Pterodontic acidBovine serum albuminFluorescence quenchingSynchronous fluorescenceThree-dimensional fluorescenceDynamic light scattering |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yunfang Li Guangzhong Yang Zhinan Mei |
spellingShingle |
Yunfang Li Guangzhong Yang Zhinan Mei Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin Acta Pharmaceutica Sinica B Pterodontic acid Bovine serum albumin Fluorescence quenching Synchronous fluorescence Three-dimensional fluorescence Dynamic light scattering |
author_facet |
Yunfang Li Guangzhong Yang Zhinan Mei |
author_sort |
Yunfang Li |
title |
Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin |
title_short |
Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin |
title_full |
Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin |
title_fullStr |
Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin |
title_full_unstemmed |
Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin |
title_sort |
spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin |
publisher |
Elsevier |
series |
Acta Pharmaceutica Sinica B |
issn |
2211-3835 2211-3843 |
publishDate |
2012-02-01 |
description |
Pterodontic acid (PA) has been isolated from Laggera pterodonta, a Chinese herbal medicine, and shown to possess antibacterial activity in vitro. To facilitate its preclinical development, the interaction between PA and bovine serum albumin (BSA) was studied using a fluorescence quenching technique, ultraviolet–visible spectrophotometry and dynamic light scattering (DLS). At temperatures of 297 K and 310 K and an excitation wavelength of 282 nm, the fluorescence intensity of BSA decreased significantly with increasing concentration of PA attributed to the formation of a PA–BSA complex. The apparent binding constant, number of binding sites and corresponding thermodynamic parameters were calculated and the main intermolecular attraction shown to result from hydrogen bonding and van der Waals forces. Synchronous fluorescence spectrometry revealed that the binding site in the complex approached the microenvironment of Trp and three-dimensional fluorescence spectroscopy showed the binding induced conformational changes in BSA. Using DLS, increasing PA concentration was shown to cause a gradual increase in hydrodynamic diameter and significant aggregation of the complex. |
topic |
Pterodontic acid Bovine serum albumin Fluorescence quenching Synchronous fluorescence Three-dimensional fluorescence Dynamic light scattering |
url |
http://www.sciencedirect.com/science/article/pii/S2211383511001031 |
work_keys_str_mv |
AT yunfangli spectroscopicanddynamiclightscatteringstudiesoftheinteractionbetweenpterodonticacidandbovineserumalbumin AT guangzhongyang spectroscopicanddynamiclightscatteringstudiesoftheinteractionbetweenpterodonticacidandbovineserumalbumin AT zhinanmei spectroscopicanddynamiclightscatteringstudiesoftheinteractionbetweenpterodonticacidandbovineserumalbumin |
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