High-resolution structure of proIAPP(1–48) fibrils suggests a mechanistic pathway for diabetes-associated IAPP fibril polymorphs

2025/10/31 by Dylan Valli, Michał Maj · 1 voice
Medicine · Biochemistry, Genetics and Molecular Biology · Materials Science · #Alzheimer's disease research and treatments #Amyloidosis: Diagnosis, Treatment, Outcomes #Supramolecular Self-Assembly in Materials

paper · pdf · doi:10.1039/d5cb00228a

openalex created_date 2025/10/31 · openalex publication_date 2025/10/31 · openalex updated_date 2026/08/01

Abstract

Structure of misprocessed proIAPP(1–48) shows how processing errors may bias hIAPP toward disease-relevant folds.

Citations

• GROMACS: A message-passing parallel molecular dynamics implementation
• The missing term in effective pair potentials

Discussions

• 🔎How does seeding by proIAPP influence amyloid fibril structure in type 2 diabetes? Find out in the latest #openaccess Advance Article from Dylan Valli and Michal Maj at Uppsala University @uu.se ➡ [bsky, 0 points, 0 comments]