ArticleBiochemical and biophysical research communications2026
Solution NMR reveals micelle-stabilized α-helical segments flanking the RIPK1 RHIM amyloid core.
Article in Biochemical and biophysical research communications, 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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Abstract
Receptor Interacting Protein Kinase 1 (RIP1 or RIPK1) can transition from a monomeric state to amyloid assemblies during cell signaling via a conserved RIP homotypic interaction motif (RHIM). Through RHIM-RHIM interactions, RIPK1 forms both homomeric and heteromeric amyloids implicated in programmed cell death, but solution-state characterization of unassembled RIPK1 is hindered by rapid aggregation. Building on our recent RIPK1 fibril structure, we designed an aggregation-slowing mutant (N545D) and show that two segments within RIPK1's disordered domain display nascent helical propensity under near-physiological pH conditions. SDS micelles further stabilize these helices and enable measurements on the wild-type sequence. Notably, analogous conditions do not reveal comparable α-helical populations in RIPK3, despite a conserved RHIM sequence and amyloid structure endpoint.
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