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Effect of C-Terminal Amidation on Folding and Disulfide-Pairing of α-Conotoxin ImI

Authors

  • Tse Siang Kang,

    1. Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Block S3 #03–17, Singapore 117543, Singapore, Fax: (+65) 6779–2486
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  • Subramanian Vivekanandan Dr.,

    1. Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Block S3 #03–17, Singapore 117543, Singapore, Fax: (+65) 6779–2486
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  • Seetharama D. S. Jois Dr.,

    1. Department of Pharmacy, National University of Singapore, Singapore 117543, Singapore
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  • R. Manjunatha Kini Prof.

    1. Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Block S3 #03–17, Singapore 117543, Singapore, Fax: (+65) 6779–2486
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  • This work is supported by the Biomedical Research Council, Agency for Science, Technology, and Research, Singapore. T.S.K. acknowledges the Singapore Millennium Foundation for granting the research scholarship. The authors thank the Sophisticated Instrument Facility at the Indian Institute of Science and the Chemical and Molecular Analysis Center, Department of Chemistry at the National University of Singapore for allowing the use of their NMR spectrometers.

Abstract

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Building bridges: α-Conotoxins (C1–C3, C2–C4 disulfide pairing) adopt a globular conformation, whereas χ/λ-conotoxins (C1–C4, C2–C3 disulfide pairing) fold into a ribbon conformation. Amidation of the peptide C terminus has been shown to influence the folding (see picture) and hence the biological activity of conotoxins.

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