pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2022

pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils

Christin Pohl
Gregory Effantin
Guy Schoehn
Allan Noergaard

Résumé

Abstract Self-assembly and fibril formation play important roles in protein behaviour. Amyloid fibril formation is well-studied due to its role in neurodegenerative diseases and characterized by refolding of the protein into predominantly β-sheet form. However, much less is known about the assembly of proteins into other types of supramolecular structures. Using cryo-electron microscopy at a resolution of 1.97 Å, we show that a triple-mutant of the anti-microbial peptide plectasin, PPI42, assembles into helical non-amyloid fibrils. The in vitro anti-microbial activity was determined and shown to be enhanced compared to the wildtype. Plectasin contains a cysteine-stabilised α-helix-β-sheet structure, which remains intact upon fibril formation. Two protofilaments form a right-handed protein fibril. The fibril formation is reversible and follows sigmoidal kinetics with a pH- and concentration dependent equilibrium between soluble monomer and protein fibril. This high-resolution structure reveals that α/β proteins can natively assemble into fibrils.

Dates et versions

hal-03917586 , version 1 (02-01-2023)

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Citer

Christin Pohl, Gregory Effantin, Eaazhisai Kandiah, Sebastian Meier, Guanghong Zeng, et al.. pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils. Nature Communications, 2022, 13 (1), pp.3162. ⟨10.1038/s41467-022-30462-w⟩. ⟨hal-03917586⟩
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