Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme

Josephine W. Wu, Kuan Nan Liu, Su Chun How, Wei An Chen, Chia Min Lai, Hwai Shen Liu, Chaur Jong Hu, Steven S S Wang

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35 Citations (Scopus)

Abstract

Carnosine, a common dipeptide in mammals, has previously been shown to dissemble alpha-crystallin amyloid fibrils. To date, the dipeptide's anti-fibrillogensis effect has not been thoroughly characterized in other proteins. For a more complete understanding of carnosine's mechanism of action in amyloid fibril inhibition, we have investigated the effect of the dipeptide on lysozyme fibril formation and induced cytotoxicity in human neuroblastoma SH-SY5Y cells. Our study demonstrates a positive correlation between the concentration and inhibitory effect of carnosine against lysozyme fibril formation. Molecular docking results show carnosine's mechanism of fibrillogenesis inhibition may be initiated by binding with the aggregation-prone region of the protein. The dipeptide attenuates the amyloid fibril-induced cytotoxicity of human neuronal cells by reducing both apoptotic and necrotic cell deaths. Our study provides solid support for carnosine's amyloid fibril inhibitory property and its effect against fibril-induced cytotoxicity in SH-SY5Y cells. The additional insights gained herein may pave way to the discovery of other small molecules that may exert similar effects against amyloid fibril formation and its associated neurodegenerative diseases.

Original languageEnglish
Article numbere81982
JournalPLoS One
Volume8
Issue number12
DOIs
Publication statusPublished - Dec 11 2013

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

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    Wu, J. W., Liu, K. N., How, S. C., Chen, W. A., Lai, C. M., Liu, H. S., Hu, C. J., & Wang, S. S. S. (2013). Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme. PLoS One, 8(12), [e81982]. https://doi.org/10.1371/journal.pone.0081982