Capsaicin inhibits collagen fibril formation and increases the stability of collagen fibers

Capsaicin is a versatile plant product which has been ascribed several health benefits and anti-inflammatory and analgesic properties. We have investigated the effect of capsaicin on the molecular stability, self-assembly, and fibril stability of type-I collagen. It was found that capsaicin suppress...

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Bibliographic Details
Published in:European biophysics journal 2015-02, Vol.44 (1-2), p.69-76
Main Authors: Perumal, Sathiamurthi, Dubey, Kriti, Badhwar, Rahul, George, Kodimattan Joseph, Sharma, Rakesh Kumar, Bagler, Ganesh, Madhan, Balaraman, Kar, Karunakar
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biochemistry
Biodegradation
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Capsaicin - chemistry
Capsaicin - pharmacology
Cell Biology
Collagen
Enzymes
Fibers
Fibrillar Collagens - chemistry
Fibrillar Collagens - metabolism
Life Sciences
Male
Membrane Biology
Molecular Docking Simulation
Molecular Sequence Data
Nanotechnology
Neurobiology
Original Paper
Protein Binding
Protein Stability
Proteolysis
Rats
Rats, Wistar
Tendons
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Summary:Capsaicin is a versatile plant product which has been ascribed several health benefits and anti-inflammatory and analgesic properties. We have investigated the effect of capsaicin on the molecular stability, self-assembly, and fibril stability of type-I collagen. It was found that capsaicin suppresses collagen fibril formation, increases the stability of collagen fibers in tendons, and has no effect on the molecular stability of collagen. Turbidity assay data show that capsaicin does not promote disassembly of collagen fibrils. However, capsaicin moderately protects collagen fibrils from enzymatic degradation. Computational studies revealed the functions of the aromatic group and amide region of capsaicin in the collagen–capsaicin interaction. The results may have significant implications for capsaicin-based therapeutics that target excess collagen accumulation-linked pathology, for example thrombosis, fibrosis, and sclerosis.
ISSN:0175-7571
1432-1017
DOI:10.1007/s00249-014-1002-9