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Label-free nonenzymatic glycation monitoring of collagen scaffolds in type 2 diabetic mice by confocal Raman microspectroscopy
Journal article   Open access   Peer reviewed

Label-free nonenzymatic glycation monitoring of collagen scaffolds in type 2 diabetic mice by confocal Raman microspectroscopy

Panpan Shi, Hanping Liu, Xiaoyuan Deng, Ying Jin, Qiannan Wang, Hao Liu, Maosheng Chen and Xue Han
Journal of biomedical optics, v 20(2), pp 027002-027002
01 Feb 2015
PMID: 25671672
url
https://doi.org/10.1117/1.JBO.20.2.027002View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze) Open

Abstract

Biochemical Research Methods Biochemistry & Molecular Biology Life Sciences & Biomedicine Optics Physical Sciences Radiology, Nuclear Medicine & Medical Imaging Science & Technology
Collagen is the key target of nonenzymatic glycation during physiopathological processes such as diabetes. The induced changes in the biochemical property of collagen by nonenzymatic glycation remain a major challenge to probe. This study investigated the use of confocal Raman microspectroscopy to label-free monitor the nonenzymatic glycation of collagen scaffolds from type 2 diabetic (T2D) mice at different timepoints (0, 4, 8, and 12 weeks). The glycated collagen scaffolds were obtained through the decellularized dermal matrix method to remove the epidermis layer, subcutaneous tissue, and cells in the dermis and to retain the collagen fibrils. Raman spectra showed no changes in Raman peak positions, which indicated that nonenzymatic glycation could produce no significant changes in the triple-helix structure of collagen in T2D mice. However, the relative intensity of the Raman bands at 921, 1033, 1244, 1274, 1346, 1635, and 1672 cm(-1) increased as diabetic time progressed. Correlation analysis suggested that the spectra of these bands had a high positive correlation with the expression of anti-advanced glycation end products obtained by immunofluorescence imaging of the same collagen scaffolds. Confocal Raman microspectroscopy proves a potential tool to label-free monitor the collagen changes caused by nonenzymatic glycation in T2D mice. (C) 2015 Society of Photo-Optical Instrumentation Engineers (SPIE)

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Web of Science research areas
Biochemical Research Methods
Optics
Radiology, Nuclear Medicine & Medical Imaging
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