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Title: Determination of Protein by Fluorescence Enhancement of Curcumin in Lanthanum-Curcumin-Sodium Dodecyl Benzene Sulfonate-Protein System

Abstract

We found that the fluorescence intensity of the lanthanum (La(3+))-curcumin (CU) complex can be highly enhanced by proteins in the presence of sodium dodecyl benzene sulphonate (SDBS). Based on this finding, a new fluorimetric method for the determination of protein was developed. Under optimized conditions, the enhanced intensities of fluorescence are quantitatively in proportion to the concentrations of proteins in the range 0.0080-20.0 g mL(-1) for bovine serum albumin (BSA) and 0.00080-20.0 g mL(-1) for human serum albumin (HSA) with excitation of 425 nm, and 0.00020-20.0 g mL(-1) for bovine serum albumin (BSA) and 0.00080-20.0 g mL(-1)for human serum albumin (HSA) with excitation of 280 nm, while corresponding qualitative detection limits (S/N 3) are as low as 5.368, 0.573, 0.049, 0.562 g mL(-1), respectively. Study on reaction mechanism reveals that proteins can bind with La(3+), CU and SDBS through self-assembling function with electrostatic attraction, hydrogen bonding, hydrophobic interaction and van der Waals forces, etc. The proteins form a supermolecular association with multilayer structure, in which La(3+)-CU is clamped between BSA and SDBS. The unique high fluorescence enhancement of CU is resulted through synergic effects of favorable hydrophobic microenvironment provided by BSA and SDBS, and efficient intermolecular energy transfer among BSA,more » SDBS and CU. In energy transfer process, La(3+) plays a crucial role because it not only shortens the distance between SDBS and CU, but also acts as a "bridge" for transferring the energy from BSA to CU.« less

Authors:
 [1];  [1];  [1];  [1];  [1];  [2];  [3]
  1. Zaozhuang University, People's Republic of China
  2. Shandong University, Jinan, China
  3. ORNL
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Oak Ridge National Environmental Research Park
Sponsoring Org.:
USDOE
OSTI Identifier:
1015087
DOE Contract Number:  
DE-AC05-00OR22725
Resource Type:
Journal Article
Journal Name:
Journal of Fluorescence
Additional Journal Information:
Journal Volume: 21; Journal Issue: 1; Journal ID: ISSN 1053--0509
Country of Publication:
United States
Language:
English
Subject:
08 HYDROGEN; ALBUMINS; BENZENE; BLOOD SERUM; BONDING; CATTLE; CURCUMIN; ELECTROSTATICS; ENERGY TRANSFER; EXCITATION; FLUORESCENCE; HYDROGEN; LANTHANUM; PROTEINS; REACTION KINETICS; SENSITIVITY; SODIUM; VAN DER WAALS FORCES

Citation Formats

Wang, Feng, Huang, Wei, Zhang, Yunfeng, Wang, Mingyin, Sun, Lina, Tang, Bo, and Wang, Wei. Determination of Protein by Fluorescence Enhancement of Curcumin in Lanthanum-Curcumin-Sodium Dodecyl Benzene Sulfonate-Protein System. United States: N. p., 2011. Web. doi:10.1007/s10895-010-0686-1.
Wang, Feng, Huang, Wei, Zhang, Yunfeng, Wang, Mingyin, Sun, Lina, Tang, Bo, & Wang, Wei. Determination of Protein by Fluorescence Enhancement of Curcumin in Lanthanum-Curcumin-Sodium Dodecyl Benzene Sulfonate-Protein System. United States. https://doi.org/10.1007/s10895-010-0686-1
Wang, Feng, Huang, Wei, Zhang, Yunfeng, Wang, Mingyin, Sun, Lina, Tang, Bo, and Wang, Wei. 2011. "Determination of Protein by Fluorescence Enhancement of Curcumin in Lanthanum-Curcumin-Sodium Dodecyl Benzene Sulfonate-Protein System". United States. https://doi.org/10.1007/s10895-010-0686-1.
@article{osti_1015087,
title = {Determination of Protein by Fluorescence Enhancement of Curcumin in Lanthanum-Curcumin-Sodium Dodecyl Benzene Sulfonate-Protein System},
author = {Wang, Feng and Huang, Wei and Zhang, Yunfeng and Wang, Mingyin and Sun, Lina and Tang, Bo and Wang, Wei},
abstractNote = {We found that the fluorescence intensity of the lanthanum (La(3+))-curcumin (CU) complex can be highly enhanced by proteins in the presence of sodium dodecyl benzene sulphonate (SDBS). Based on this finding, a new fluorimetric method for the determination of protein was developed. Under optimized conditions, the enhanced intensities of fluorescence are quantitatively in proportion to the concentrations of proteins in the range 0.0080-20.0 g mL(-1) for bovine serum albumin (BSA) and 0.00080-20.0 g mL(-1) for human serum albumin (HSA) with excitation of 425 nm, and 0.00020-20.0 g mL(-1) for bovine serum albumin (BSA) and 0.00080-20.0 g mL(-1)for human serum albumin (HSA) with excitation of 280 nm, while corresponding qualitative detection limits (S/N 3) are as low as 5.368, 0.573, 0.049, 0.562 g mL(-1), respectively. Study on reaction mechanism reveals that proteins can bind with La(3+), CU and SDBS through self-assembling function with electrostatic attraction, hydrogen bonding, hydrophobic interaction and van der Waals forces, etc. The proteins form a supermolecular association with multilayer structure, in which La(3+)-CU is clamped between BSA and SDBS. The unique high fluorescence enhancement of CU is resulted through synergic effects of favorable hydrophobic microenvironment provided by BSA and SDBS, and efficient intermolecular energy transfer among BSA, SDBS and CU. In energy transfer process, La(3+) plays a crucial role because it not only shortens the distance between SDBS and CU, but also acts as a "bridge" for transferring the energy from BSA to CU.},
doi = {10.1007/s10895-010-0686-1},
url = {https://www.osti.gov/biblio/1015087}, journal = {Journal of Fluorescence},
issn = {1053--0509},
number = 1,
volume = 21,
place = {United States},
year = {Sat Jan 01 00:00:00 EST 2011},
month = {Sat Jan 01 00:00:00 EST 2011}
}