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Amyloid Fibrils03:03

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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. 
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

Updated: Nov 22, 2025

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
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AL Amyloidosis: Unfolding a Complex Disease.

Rebecca Lu1, Tiffany A Richards1

  • 1The University of Texas MD Anderson Cancer Center, Houston, Texas.

Journal of the Advanced Practitioner in Oncology
|January 11, 2021
PubMed
Summary

Light chain (AL) amyloidosis is a rare plasma cell disorder where misfolded proteins damage organs. Recent treatment advancements offer hope for patients with this progressive condition.

Area of Science:

  • Hematology
  • Oncology
  • Nephrology

Background:

  • Light chain (AL) amyloidosis is a rare plasma cell dyscrasia affecting approximately 12,000 individuals in the U.S.
  • The disease results from the misfolding and deposition of proteins in vital organs, including the heart, kidneys, and nervous system.
  • Organ damage leads to progressive impairment and reduced quality of life for affected individuals.

Purpose of the Study:

  • To provide a comprehensive overview of AL amyloidosis.
  • To detail the pathophysiology, diagnostic approaches, and current treatment strategies for AL amyloidosis.
  • To highlight recent advancements and ongoing developments in AL amyloidosis therapy.

Main Methods:

  • Literature review of pathophysiology, diagnosis, and treatment of AL amyloidosis.

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  • Analysis of current therapeutic options and emerging treatments.
  • Synthesis of information on disease mechanisms and clinical management.

    • Main Results:

    • AL amyloidosis is characterized by the deposition of misfolded light chains, causing multi-organ dysfunction.
    • Diagnosis relies on identifying the underlying plasma cell disorder and confirming amyloid deposits.
    • Treatment has significantly improved, with novel therapies showing promise.

    Conclusions:

    • AL amyloidosis requires a multidisciplinary approach for effective management.
    • Ongoing research is crucial for developing more targeted and effective treatments.
    • Improved understanding of pathophysiology aids in earlier diagnosis and better patient outcomes.