Capsaicin inhibits collagen fibril formation and increases the stability of collagen fibers
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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.
KeywordsCapsaicin Type-I collagen Tendons Triple-helix
Rat tail tendon
We thank the Indian Institute of Technology, Jodhpur, for research facilities. We are grateful to Central Leather Research Institute, Chennai, for laboratory support with some of the biophysical studies. Authors SP and BM are grateful for CSIR-YSA grants from CSIR (CSIR-CLRI Communication number 1122). Authors KK and GB thank the Indian Institute of Technology, Jodhpur, for the Seed Grant, and author KK is grateful for BRNS [No.37(1)/14/38/2014-BRNS/1357] funding support.
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