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Sub-persistence-length complex scaling behavior in lysozyme amyloid fibrils.
Cécile Lara1, Ivan Usov, Jozef Adamcik
1ETH Zurich, Food & Soft Materials Science, Institute of Food, Nutrition & Health, Schmelzbergstrasse 9, LFO E23, 8092 Zurich, Switzerland.
Physical Review Letters
|December 21, 2011
Summary
Lysozyme amyloid fibrils exhibit a complex wavy structure with distinct bending and flexibility at multiple length scales. This conformation is influenced by fibril twisting and its impact on bending propensity.
Area of Science:
- Biophysics
- Polymer Physics
- Materials Science
Background:
- Amyloid fibrils are protein aggregates implicated in various diseases.
- Understanding their structural properties is crucial for disease mechanisms and therapeutic strategies.
Purpose of the Study:
- To investigate the molecular conformations and structural characteristics of lysozyme amyloid fibrils.
- To identify and characterize the length scales governing fibril morphology and flexibility.
Main Methods:
- Atomic force microscopy (AFM) single-molecule analysis.
- Application of polymer physics models, including the wormlike chain model.
- Analysis of bond and pair correlation functions and end-to-end distribution.
Main Results:
- Lysozyme amyloid fibrils display a wavy structure with scaling behavior varying across multiple length scales.
- Three characteristic length scales were identified: a bending transition (≈150 nm), pseudoperiodic undulation (>2L(b)), and flexibility at larger scales (> persistence length).
- Fibril twisting influences the area moment of inertia and bending propensity.
Conclusions:
- The study reveals a multi-scale structural complexity in lysozyme amyloid fibrils.
- Fibril conformation transitions from bending to undulation and finally to flexible random walk behavior.
- Fibril twisting is a key factor determining the observed structural properties and mechanical behavior.
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