Generating the polymorph landscapes of amyloid fibrils using AI: RibbonFold.

ABSTRACT: The concept that proteins are selected to fold into a well-defined native state has been effectively addressed within the framework of energy landscapes, underpinning the recent successes of structure prediction tools like AlphaFold. The amyloid fold, however, does not represent a unique minimum for a given single sequence. While the cross-β hydrogen-bonding pattern is common to all amyloids, other aspects of amyloid fiber structures are sensitive not only to the sequence of the aggregating peptides but also to the experimental conditions. This polymorphic nature of amyloid structures challenges structure predictions. In this paper, we use AI to explore the landscape of possible amyloid protofilament structures composed of a single stack of peptides aligned in a parallel, in-registe

SUBMITTER: Guo L 

PROVIDER: S-EPMC12037047 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature