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Fluorescence characterization of the thermal stability of collagen mimic peptides
- Source :
- Chinese Chemical Letters. 28:963-967
- Publication Year :
- 2017
- Publisher :
- Elsevier BV, 2017.
-
Abstract
- 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.
- Subjects :
- 0301 basic medicine
Chemistry
Collectin
General Chemistry
010402 general chemistry
01 natural sciences
Fluorescence
Fluorescence spectroscopy
0104 chemical sciences
Highly sensitive
Characterization (materials science)
03 medical and health sciences
030104 developmental biology
Biochemistry
Thermal stability
Function (biology)
Triple helix
Subjects
Details
- ISSN :
- 10018417
- Volume :
- 28
- Database :
- OpenAIRE
- Journal :
- Chinese Chemical Letters
- Accession number :
- edsair.doi...........6163a1e1df2ef26e05dfd8c27c7acdc0