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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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Related Experiment Video

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Capping effects on polymorphic Aβ_16-21 amyloids depend on their size: A molecular dynamics simulation study.

Myeongsang Lee¹, Hyun Joon Chang², Hyunsung Choi²

¹Institute of Advanced Machinery Design and Technology, Korea University, 02841 Seoul, Republic of Korea.

Biophysical Chemistry

|October 20, 2017

Summary

Terminal capping alters amyloid oligomer structure and stability, but not protofibrils. Electrostatic energy significantly impacts Aβ_16-21 amyloid stability, offering insights for drug design.

Keywords:

Amyloids Aβ Capping effect Molecular dynamics (MD)Polymorphism

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Published on: July 14, 2010

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Published on: July 14, 2010

Area of Science:

Neuroscience
Biochemistry
Computational Biology

Background:

Amyloid oligomers are implicated in neurodegenerative diseases due to their toxicity and role in fibril formation.
Amyloid structures exhibit polymorphism influenced by factors like ionic strength and mutations.
Terminal capping affects amyloid properties, but its role in polymorphic structures remains unclear.

Purpose of the Study:

To investigate the impact of N-terminal acetylation and C-terminal amidation on polymorphic Aβ_16-21 amyloid oligomers and protofibrils.
To elucidate the influence of capping on the conformation and thermodynamic stability of these amyloid structures.
To understand the contribution of electrostatic energy to amyloid stability in the context of capping.

Main Methods:

Utilized molecular dynamics (MD) simulations to model Aβ_16-21 amyloid oligomers and protofibrils.
Analyzed conformational changes and thermodynamic stabilities under different capping conditions (N-terminal acetylation, C-terminal amidation).
Quantified the role of molecular mechanics, particularly electrostatic energy, in amyloid stability.

Main Results:

Terminal capping differentially altered the conformation of antiparallel-homo and -hetero Aβ_16-21 amyloid oligomers, but not protofibrils.
Capping induced thermodynamic instabilities in Aβ_16-21 amyloid oligomers, irrespective of their polymorphic composition.
No distinct effect of capping was observed on the stability of Aβ_16-21 amyloid protofibrils.
Electrostatic energy was identified as a dominant factor in the thermodynamic stability of Aβ_16-21 amyloids.

Conclusions:

Terminal capping significantly influences the structural and stability characteristics of Aβ_16-21 amyloid oligomers, but not protofibrils.
The findings highlight the critical role of electrostatic interactions in amyloid stability.
This study provides a computational basis for future therapeutic strategies targeting amyloid degradation and drug design for neurodegenerative diseases.