9GJ4

Structure of the amyloid-forming peptide LYNleQNY

Summary for 9GJ4

• Entry DOI: 10.2210/pdb9gj4/pdb
• Descriptor: Peptide LYNleQNY (2 entities in total)
• Functional Keywords: amyloid, protein fibril
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 812.91

Authors

Durvanger, Z. (deposition date: 2024-08-21, release date: 2025-07-09)

Primary citation

Bencs, F.,Taricska, N.,Durvanger, Z.,Horvath, D.,Fazekas, Z.,Grolmusz, V.,Farkas, V.,Perczel, A.
Chemical Evolution of Early Macromolecules: From Prebiotic Oligopeptides to Self-Organizing Biosystems via Amyloid Formation.
Chemistry, 31:e202404669-e202404669, 2025

PubMed Abstract: Short amyloidogenic oligopeptides (APRs) are proposed as early macromolecules capable of forming solvent-separated nanosystems under prebiotic conditions. This study provides experimental evidence that APRs, such as the aggregation-prone oligopeptide A (APR-A), can undergo mutational transitions to form distinct variants and convert to APR-B, either amyloid-like or water-soluble and non-aggregating. These transitions occur along a spectrum from strongly amyloidogenic (pro-amyloid) to weakly amyloidogenic (anti-amyloid), with the mutation sequence order playing a key role in determining their physicochemical properties. The pro-amyloid pathway facilitates heterogeneous phase separation, leading to amyloid-crystal formation with multiple polymorphs, including the first class 3 amyloid topology. By mapping these transitions, we demonstrate the potential co-evolution of water-soluble miniproteins and insoluble amyloids, both of which could have been pivotal in early bio-nanosystem formation. These insights into amyloid modulation provide a crucial step toward understanding amyloid control mechanisms.

PubMed: 40197673
DOI: 10.1002/chem.202404669

Experimental method

X-RAY DIFFRACTION (1.55 Å)