The structure of cross-ß tapes and tubes formed by an octapeptide, aSß1
journal contribution
posted on 2023-06-08, 13:33authored byKyle L Morris, Shahin Zibaee, Lin Chen, Michel Goedert, Pawel Sikorski, Louise SerpellLouise Serpell
Elaborate morphology: The aSß1 peptide, a fragment of a-synuclein, assembles into flat tapes consisting of a peptide bilayer, which can be modeled based on the cross-ß structure found in amyloid proteins. The tapes are stabilized by hydrogen bonding, whilst the amphiphilic nature of the peptide results in the thin bilayer structure. To further stabilize the structure, these tapes may twist to form helical tapes, which subsequently close into nanotubes.