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Proceedings Paper

Photoinduced structural changes to protein kinase A
Author(s): Sarah C. Rozinek; Robert J. Thomas; Lorenzo Brancaleon
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Paper Abstract

The importance of porphyrins in organisms is underscored by the ubiquitous biological and biochemical functions that are mediated by these compounds and by their potential biomedical and biotechnological applications. Protoporphyrin IX (PPIX) is the precursor to heme and has biomedical applications such as its use as a photosensitizer in phototherapy and photodetection of cancer. Among other applications, our group has demonstrated that low-irradiance exposure to laser irradiation of PPIX, Fe-PPIX, or meso-tetrakis (4-sulfonatophenyl) porphyrin (TSPP) non-covalently docked to a protein causes conformational changes in the polypeptide. Such approach can have remarkable consequences in the study of protein structure/function relationship and can be used to prompt non-native protein properties. Therefore we have investigated protein kinase A (PKA), a more relevant protein model towards the photo-treatment of cancer. PKA’s enzymatic functions are regulated by the presence of cyclic adenosine monophosphate for intracellular signal transduction involved in, among other things, stimulation of transcription, tumorigenesis in Carney complex and migration of breast carcinoma cells. Since phosphorylation is a necessary step in some cancers and inflammatory diseases, inhibiting the protein kinase, and therefore phosphorylation, may serve to treat these diseases. Changes in absorption, steady-state fluorescence, and fluorescence lifetime indicate: 1) both TSPP and PPIX non-covalently bind to PKA where they maintain photoreactivity; 2) absorptive photoproduct formation occurs only when PKA is bound to TSPP and irradiated; and 3) PKA undergoes secondary structural changes after irradiation with either porphyrin bound. These photoinduced changes could affect the protein’s enzymatic and signaling capabilities.

Paper Details

Date Published: 13 March 2014
PDF: 6 pages
Proc. SPIE 8941, Optical Interactions with Tissue and Cells XXV; and Terahertz for Biomedical Applications, 89410T (13 March 2014); doi: 10.1117/12.2038561
Show Author Affiliations
Sarah C. Rozinek, Air Force Research Lab. (United States)
The Univ. of Texas at San Antonio (United States)
Robert J. Thomas, Air Force Research Lab. (United States)
Lorenzo Brancaleon, The Univ. of Texas at San Antonio (United States)


Published in SPIE Proceedings Vol. 8941:
Optical Interactions with Tissue and Cells XXV; and Terahertz for Biomedical Applications
E. Duco Jansen; Gerald J. Wilmink; Bennett L. Ibey; Robert J. Thomas, Editor(s)

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