ArticleBiochemistry2026
N-Terminal Amine Chemistry Influences α-Synuclein Interactions with Lipid Bilayers.
Article in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
α-Synuclein (αSyn) is an intrinsically disordered protein whose reversible membrane binding via amphipathic α-helix formation is central to its function and may also contribute to the pathology of Parkinson's disease. In mammals, αSyn is constitutively N-terminally acetylated, a modification that alters its structural propensity and interactions with lipid bilayers. Here, we decouple the structural and chemical contributions of N-terminal acetylation by engineering several αSyn variants that systematically vary N-terminal helix propensity and physicochemical properties: unmodified αSyn (αSyn
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