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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: Jun 20, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Challenges in Peptide Solubilization - Amyloids Case Study.

Oliwia Polańska¹, Natalia Szulc², Rafał Stottko³

¹Department of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wroclaw University of Science and Technology, Wybrzeze Wyspianskiego 27, 50-370, Wroclaw, Poland.

Chemical Record (New York, N.Y.)

|July 18, 2024

Summary

This summary is machine-generated.

Peptide solubility is a major challenge in drug development. This review explores reasons for poor peptide solubility and analyzes strategies for dissolving difficult peptide sequences, including amyloids.

Keywords:

Aggregation dissolution monomerization solubility “difficult sequences”

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Last Updated: Jun 20, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

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Published on: December 5, 2013

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

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Published on: July 16, 2008

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Area of Science:

Peptide science
Biochemistry
Drug development

Background:

Peptides offer significant potential in medicine due to their biocompatibility and bioactivity.
Low solubility is a primary obstacle hindering peptide drug development, impacting their behavior and application.
Understanding and overcoming solubility issues are critical for advancing peptide-based therapeutics.

Purpose of the Study:

To investigate the underlying causes of peptide dissolution difficulties.
To critically analyze existing strategies and protocols for peptide solubilization.
To provide practical guidance for handling challenging peptide sequences, particularly amyloids.

Main Methods:

Literature review and critical analysis of published data on peptide solubility.
Examination of factors contributing to peptide aggregation.
Focus on specific amyloid peptides like amyloid beta (Aβ), insulin, and phenol-soluble modulins (PSMs).

Main Results:

Peptide solubility is complex and influenced by multiple factors, with no universal solubilization method.
Peptide aggregation, especially in amyloids, presents significant challenges for dissolution and handling.
Existing protocols vary in effectiveness and are often sequence-specific.

Conclusions:

Addressing peptide solubility requires a nuanced approach, considering sequence-specific properties and aggregation tendencies.
Further research into novel solubilization techniques is needed to fully realize the therapeutic potential of peptides.
Effective strategies for dissolving difficult peptides, like amyloids, are crucial for successful drug development.