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Updated: Jul 17, 2026

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis
Published on: August 7, 2018
Evaluation of biologically relevant short alpha-helices stabilized by a main-chain hydrogen-bond surrogate
Deyun Wang1, Kang Chen, John L Kulp Iii
1Department of Chemistry, New York University, New York, New York 10003, USA.
Abstract:
We previously reported the design and synthesis of a new class of artificial alpha-helices in which an N-terminal main-chain hydrogen bond is replaced by a carbon-carbon bond derived from a ring-closing metathesis reaction [Chapman, R. N.; Dimartino, G.; Arora, P. S. J. Am. Chem. Soc. 2004, 126, 12252-12253]. Our initial study utilized an alanine-rich sequence; in the present manuscript we evaluate the potential of this method for the synthesis of very short (10 residues) alpha-helices representing two different biologically relevant alpha-helical domains. We extensively characterized these two sets of artificial helices by NMR and circular dichroism spectroscopies and find that the hydrogen-bond surrogate approach can afford well-defined short alpha-helical structures from sequences that do not spontaneously form alpha-helical conformations.
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