Open AccessDecrease in fluorescence lifetime by glycation of collagen and its application in determining advanced glycation end-products in human dentin
Author(s) -
Shuichiro Fukushima,
Masato Shimizu,
Jiro Miura,
Yusuke Matsuda,
Mizuho Kubo,
Mamoru Hashimoto,
Takuya Aoki,
Fumio Takeshige,
Tsutomu Araki
Publication year - 2015
Publication title -
biomedical optics express
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.362
H-Index - 86
ISSN - 2156-7085
DOI - 10.1364/boe.6.001844
Subject(s) - glycation , fluorescence , maillard reaction , chemistry , dentin , in vivo , fluorescence spectroscopy , biophysics , biochemistry , pathology , biology , optics , medicine , physics , receptor , microbiology and biotechnology
Advanced Glycation End-products (AGEs) are produced by the Maillard reaction, which causes cross-linking of collagen and results in changes in the mechanical properties of collagen tissues. Several types of AGE fluoresce, and measurement of this fluorescence is effective for determining the presence of AGEs. Because fluorescence intensity by steady-state fluorometry is affected by sample surface condition and light source, we focused on fluorescence lifetime measurement (FLM). We found that fluorescence lifetime of collagen gel decreased with glycation progress. In vivo application of FLM for determination of AGEs was confirmed in human dentin.