8GI5

Cryo-EM of self-assembling pyrene peptide with Ca2+

Summary for 8GI5

• Entry DOI: 10.2210/pdb8gi5/pdb
• EMDB information: 40061
• Descriptor: Pyrene peptide (1 entity in total)
• Functional Keywords: peptides, nanofibers, self-assembly peptide filament, protein fibril
• Biological source: synthetic construct
• Total number of polymer chains: 4
• Total formula weight: 4240.03

Authors

Rich-New, S.T.,Guo, J.,Xu, B.,Wang, F. (deposition date: 2023-03-13, release date: 2023-06-14, Last modification date: 2024-10-16)

Primary citation

Guo, J.,Rich-New, S.T.,Liu, C.,Huang, Y.,Tan, W.,He, H.,Yi, M.,Zhang, X.,Egelman, E.H.,Wang, F.,Xu, B.
Hierarchical Assembly of Intrinsically Disordered Short Peptides.
Chem, 9:2530-2546, 2023

PubMed Abstract: 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.

PubMed: 38094164
DOI: 10.1016/j.chempr.2023.04.023

Experimental method

ELECTRON MICROSCOPY (3 Å)