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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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Updated: Apr 30, 2026

Author Spotlight: A Live Cell Imaging Technique to Study Calcium Signaling and Acrosome Exocytosis in Mouse Sperm

Author Spotlight: A Live Cell Imaging Technique to Study Calcium Signaling and Acrosome Exocytosis in Mouse Sperm

Published on: October 13, 2023

Functional amyloids in the mouse sperm acrosome.

Benoit Guyonnet, Nathan Egge, Gail A Cornwall

Molecular and Cellular Biology

|May 7, 2014

Summary

Sperm acrosomal matrix stability is due to amyloid structures. These amyloids, crucial for sperm-zona pellucida interaction, disassemble at pH 7, facilitating the acrosome reaction.

Area of Science:

Reproductive Biology
Biochemistry
Sperm Biology

Background:

The sperm acrosomal matrix (AM) is an insoluble scaffold essential for sperm function.
Its stability, particularly during the acrosome reaction, is poorly understood.
The AM interacts with the zona pellucida (ZP), a crucial step in fertilization.

Purpose of the Study:

To investigate the molecular basis of sperm acrosomal matrix stability.
To determine the role of amyloids in AM structure and function.
To elucidate the mechanism of AM dispersion during the acrosome reaction.

Main Methods:

Proteomic analysis of the sperm acrosomal matrix.
Amyloid detection assays (e.g., resistance to SDS and formic acid).

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Fluorimetric Techniques for the Assessment of Sperm Membranes

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

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Fluorimetric Techniques for the Assessment of Sperm Membranes

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pH-dependent stability studies of the AM and its amyloid core.

Main Results:

Amyloid structures are present within the sperm acrosomal matrix, forming an SDS- and formic-acid-resistant core.
The AM core comprises known and predicted amyloidogenic proteins, including ZP-binding proteins.
The AM is stable at pH 3 but rapidly disperses at pH 7, with a corresponding change in amyloid structure.

Conclusions:

Amyloids form a stable core within the sperm acrosomal matrix, contributing to its structural integrity.
The amyloid core plays a functional role in sperm-zona pellucida interactions.
pH-dependent amyloid structural changes mediate the dispersion of the acrosomal matrix during the acrosome reaction.