Unravelling the Complexity of Amyloid Peptide Core Interfaces.

ABSTRACT: Amyloids, large intermolecular sandwiched β-sheet structures, underlie several protein misfolding diseases but have also been shown to have functional roles and can be a basis for designing smart and responsive nanomaterials. Short segments of proteins, called aggregation-prone regions (APRs), have been identified that nucleate amyloid formation. Here we present the database of 173 APR crystal structures currently available in the PDB, and a tool, ACW, for analyzing their topologies and the 267 inter-β-sheet interfaces of zipper regions assigned in these structures. We defined a new descriptor of zipper interfaces, the surface detail index (SDi), which quantifies the intertwining between the side chains of both β-sheets of the zipper, an important factor for the molecular recognition and s

SUBMITTER: Sulyok-Eiler M 

PROVIDER: S-EPMC11600497 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature