Citation: Sun Xiu-Xia, Fan Jun, Hou Yan-Nan, Liang Shuo, Zhang Yu-Ping, Xiao Jian-Xi. Fluorescence characterization of the thermal stability of collagen mimic peptides[J]. Chinese Chemical Letters, ;2017, 28(5): 963-967. doi: 10.1016/j.cclet.2016.11.029 shu

Fluorescence characterization of the thermal stability of collagen mimic peptides

Sun Xiu-Xia ^a,b ,
Fan Jun ^a,1 ,
Hou Yan-Nan ^a,1 ,
Liang Shuo ^a ,
Zhang Yu-Ping ^a ,
Xiao Jian-Xi ^a,b,,

a.
State Key Laboratory of Applied Organic Chemistry, Key Laboratory of Nonferrous Metal Chemistry and Resources Utilization of Gansu Province, College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou 730000, China
b.
Key laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, Hubei 430071, China

Corresponding author: Xiao Jian-Xi, xiaojx@lzu.edu.cn

Received Date: 8 August 2016
Revised Date: 9 November 2016
Accepted Date: 17 November 2016
Available Online: 28 May 2016

Figures(3)

The thermal stability of triple helical structure plays a critical role in collagen biosynthesis, function and degradation. CD technique was utilized to characterize the thermal stability of synthetic collagen mimic peptides. Fluorescence spectroscopy is widely used with easy access all around the world because of its inexpensive instrumentation, low operation cost, easy operation, and high sensitivity. Here we have developed an alternative fluorescence method to detect the thermal stability of collagen mimic peptides. We have demonstrated that fluorescence spectroscopy could measure the thermal stability of collagen mimic peptides with low concentrations under different circumstances. This highly sensitive fluorescence self-quenching assay will greatly expedite the studies of sequence-dependent properties of collagen mimic peptides, and it has great potential in the application of determining the thermal stability of triple helix systems such as collagens, collectins, adiponectin, macrophage scavenger and C1q.
- Collagen,
- Peptides,
- Thermal stability,
- Fluorescence,
- Triple helix
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