Paper
27 October 2006 Enhancement mechanism of FCLA-1O2 chemiluminescence by human serum albumin
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Proceedings Volume 6047, Fourth International Conference on Photonics and Imaging in Biology and Medicine; 60473G (2006) https://doi.org/10.1117/12.710725
Event: Fourth International Conference on Photonics and Imaging in Biology and Medicine, 2005, Tianjin, China
Abstract
Fluoresceinyl Cypridina Lucifenn Analog (FCLA) is a reactive oxygen species (ROS) specific chemiluminescence (CL) probe. Its detection efficiency of singlet oxygen (102)couldbe significantly enhanced in the presence of human serum albumin (HSA). The enhancement mechanism of HSA-FCLA CL is studied in the current work by means ofdirect CL measurement and spectroscopy. The results show that, FCLA can combine with HSA. HSA is an effective 1O2 quencher. It can react with 102 and produce a protein carbonyl group with an elevated energy state. The HSA protein carbonyl group can transfer its energy to FCLA in the FCLA-HSA complex. Via this irradiative de-excitation pathway of the excited FCLA, luminescence production from FCLA is greatly enhanced, in addition to the chemiluminescence from the direct interaction of FCLA and 102 FCLA has been reported for cancer diagnosis in vivo. Considering HSA is a natural protein that is present in all parts of a human body, the efficacy of FCLA used in vivo is expected to be enhanced through the coupling of FCLA and HSA.
© (2006) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Jing Zhou, Da Xing, and Qun Chen "Enhancement mechanism of FCLA-1O2 chemiluminescence by human serum albumin", Proc. SPIE 6047, Fourth International Conference on Photonics and Imaging in Biology and Medicine, 60473G (27 October 2006); https://doi.org/10.1117/12.710725
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KEYWORDS
Proteins

Luminescence

Chemiluminescence

Oxygen

Absorption

Spectroscopy

Analog electronics

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