# Conformational Plasticity in Amyloid Assemblies: A Paradigm Shift from Structural Rigidity to Functional Adaptability

**Authors:** Alan H. Weible, Xiaoguang Wang

PMC · DOI: 10.1021/acscentsci.5c00983 · ACS Central Science · 2025-06-06

## TL;DR

This paper shows how amyloid assemblies can change shape, challenging the idea that they are structurally rigid and suggesting they can adapt functionally.

## Contribution

The study introduces a new perspective on amyloid assemblies by demonstrating their conformational plasticity using advanced imaging techniques.

## Key findings

- hIAPP conformational ensembles vary with mutations and PTMs.
- Scanning tunneling microscopy reveals structural diversity in amyloid assemblies.
- Findings suggest amyloid assemblies are functionally adaptable rather than rigid.

## Abstract

The
divergence of conformational ensembles of hIAPP in response to different
types of mutations and PTMs has been decoded by leveraging
the scanning tunneling microscopy-based probability interpretation
technique.

## Full-text entities

- **Genes:** IAPP (islet amyloid polypeptide) [NCBI Gene 3375] {aka DAP, IAP}
- **Diseases:** Alzheimer's (MESH:D000544), prion diseases (MESH:D017096), amyloidosis (MESH:D000686), neurodegeneration (MESH:D019636), type 2 diabetes (MESH:D003924), amyloid (MESH:C000718787)
- **Species:** Homo sapiens (human, species) [taxon 9606]
- **Mutations:** S20, S20G, R18H

## Full text

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## Figures

2 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12221075/full.md

## References

6 references — full list in the complete paper: https://tomesphere.com/paper/PMC12221075/full.md

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Source: https://tomesphere.com/paper/PMC12221075