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  • Title: De novo design of a stable N-terminal helical foldamer.
    Author: Nicoll AJ, Weston CJ, Cureton C, Ludwig C, Dancea F, Spencer N, Smart OS, Günther UL, Allemann RK.
    Journal: Org Biomol Chem; 2005 Dec 21; 3(24):4310-5. PubMed ID: 16327890.
    Abstract:
    A peptide NTH-18 was synthesized in which a N-terminal helix is stabilised by two crossed disulfide bonds to a C-terminal extension. The design was inspired by the structure of the neurotoxic peptide apamin, which has previously been used to stabilise helices in miniature enzymes. CD- and NMR-spectroscopy indicated that NTH-18 adopted a fold similar to that found in apamin. However, the arrangement of the elements of secondary structures was inverted relative to apamin; a N-terminal alpha-helix was connected by a reverse turn to a C-terminal extension of non-canonical secondary structure. NTH-18 displayed significant stability to heat and changes of pH. The high definition of the N-terminal end of the alpha-helix of NTH-18 should make this peptide a useful vehicle to stabilise alpha-helices in proteins with applications in protein engineering and molecular recognition.
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