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TitleHierarchical Assembly of Intrinsically Disordered Short Peptides.
Journal, issue, pagesChem, Vol. 9, Issue 9, Page 2530-2546, Year 2023
Publish dateSep 14, 2023
AuthorsJiaqi Guo / Shane T Rich-New / Chen Liu / Yimeng Huang / Weiyi Tan / Hongjian He / Meihui Yi / Xixiang Zhang / Edward H Egelman / Fengbin Wang / Bing Xu /
PubMed AbstractThe understanding on how short peptide assemblies transit from disorder to order remains limited due to the lack of atomistic structures. Here we report cryo-EM structure of the nanofibers short ...The understanding on how short peptide assemblies transit from disorder to order remains limited due to the lack of atomistic structures. Here we report cryo-EM structure of the nanofibers short intrinsically disordered peptides (IDPs). Upon lowering pH or adding calcium ions, the IDP transitions from individual nanoparticles to nanofibers containing an aromatic core and a disordered periphery comprised of 2 to 5 amino acids. Protonating the phosphate or adding more metal ions further assembles the nanofibers into filament bundles. The assemblies of the IDP analogs with controlled chemistry, such as phosphorylation site, hydrophobic interactions, and sequences indicate that metal ions interact with the flexible periphery of the nanoparticles of the IDPs to form fibrils and enhance the interfibrillar interactions to form filament bundles. Illustrating that an IDP self-assembles from disorder to order, this work offers atomistic molecular insights to understand assemblies of short peptides driven by noncovalent interactions.
External linksChem / PubMed:38094164 / PubMed Central
MethodsEM (helical sym.)
Resolution3.0 - 3.1 Å
Structure data

EMDB-26800, PDB-7uuq:
Cryo-EM of self-assembling pyrene IDP
Method: EM (helical sym.) / Resolution: 3.1 Å

EMDB-40061, PDB-8gi5:
Cryo-EM of self-assembling pyrene peptide with Ca2+
Method: EM (helical sym.) / Resolution: 3.0 Å

Source
  • synthetic construct (others)
KeywordsPROTEIN FIBRIL / peptides / nanofibers / self-assembly peptide filament

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