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Investigation of near-infrared laser dye albumin complexes
Institution:1. Kelley School of Business, Indiana University, 1309 E Tenth Street, Bloomington, IN 47405-1701;2. College of Agriculture, Texas A&M University, College Station, TX 77843, U.S.A.;3. Mays Business School, Texas A&M University, College Station, TX 77843, U.S.A.;4. Neeley School of Business, Texas Christian University;1. Department of Immunology, National Clinical Research Center of Cancer, Tianjin Key Laboratory of Cancer Immunology and Biotherapy, Tianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China;2. Cancer Molecular Diagnostic Core, National Clinical Research Center of Cancer, Tianjin Key Laboratory of Cancer Prevention and Therapy, Tianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China;1. Department of Civil, Architecture and Environment, Xihua University, China;2. Division of Building Science and Technology, City University of Hong Kong, Hong Kong, China;1. Department of Medical Physics and Biomedical Nanotechnologies, V. N. Karazin Kharkiv National University, 4 Svobody Sq., Kharkiv 61022, Ukraine;2. Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, Acad. G. Bonchev str., bl. 9, 1113 Sofia, Bulgaria;3. Department of Pharmaceutical and Applied Organic Chemistry, Faculty of Chemistry and Pharmacy, Sofia University St. Kliment Ohridski, 1 blv. J. Bourchier, Sofia 1164, Bulgaria;1. Department of Cardiac Surgery, Royal Children’s Hospital, Melbourne, Victoria, Australia;2. University of Melbourne, Melbourne, Victoria, Australia;3. Murdoch Children’s Research Institute, Melbourne, Victoria, Australia
Abstract:Near-infrared (NIR) spectroscopy is used to investigate the properties of the NIR laser dye albumin complexes. The binding sites on albumins are probed using four structurally very similar NIR laser dyes, the DTTCI, DOTCI, DTDCI and DODCI. The pronounced differences observed in the NIR spectra of these dyes indicate that specific binding may occur since differences in the microenvironment of the binding area does not alone explain these changes. The DTTCI complexes with albumins showed a significant decrease in the NIR absorption while the other three dyes did not. These results suggest that the presence of the S heteroatoms as well as their distance from each other are determining factors in the observed specific binding. Dissimilarities in the NIR spectra of different albumin complexes indicate a difference in the structure of the microenvironment surrounding the NIR laser dye binding sites.
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