Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

6.8K
6.8K
Amyloid Fibrils03:03

Amyloid Fibrils

12.1K
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,...
12.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Comparison of two populations of the scorpion Centruroides mascota: venom composition and neutralization by a human recombinant antibody.

Toxicon : official journal of the International Society on Toxinology·2026
Same author

Beta Toxins Isolated from the Scorpion <i>Centruroides hirsutipalpus</i> (Scorpiones; Buthidae) Affect the Function of Sodium Channels of Mammals.

Toxins·2025
Same author

Rational design of indolyl acrylamides as antibacterial agents targeting multidrug-resistant <i>Acinetobacter baumannii</i> strains.

RSC medicinal chemistry·2025
Same author

Disparity among venom components, and morphometrics in Centruroides baergi Hoffmann, 1932, a medically relevant scorpion species from Mexico.

Toxicon : official journal of the International Society on Toxinology·2025
Same author

Understanding the structure and function of HPI, a rubber tree serine protease inhibitor, and its interaction with subtilisin.

Biochemical and biophysical research communications·2025
Same author

Biochemical and functional characterization of rMe'exLec1, a recombinant tandem-repeat lectin from the ancient marine chelicerate Limulus polyphemus.

International journal of biological macromolecules·2025
Same journal

The effects of two Leu-to-Pro substitutions, L57P and L43P, on structural and functional properties of cardiac tropomyosin.

The FEBS journal·2026
Same journal

Stimulating proteasomal degradation in human proteinopathies.

The FEBS journal·2026
Same journal

A lipid-sensitive food choice behavior influences aging outcomes from a longevity-promoting diet.

The FEBS journal·2026
Same journal

The interaction network of a rice seed-specific transcription factor OsMADS29 and the calcium sensors, calmodulin, and calmodulin-like proteins.

The FEBS journal·2026
Same journal

A large family of unusual voltage-sensing proton channels (Hv3) in mollusks.

The FEBS journal·2026
Same journal

RVB-1 and RVB-2 are stress responsive proteins in Neurospora crassa and RVB-1 interacts with the centromeric Shugoshin (SGO-1) protein.

The FEBS journal·2026
See all related articles

Related Experiment Video

Updated: Feb 23, 2026

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood
13:14

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

11.0K

Stabilizing an amyloidogenic λ6 light chain variable domain.

Oscar D Luna-Martínez1, Alejandra Hernández-Santoyo2, Myriam I Villalba-Velázquez1

  • 1Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Mexico.

The FEBS Journal
|September 13, 2017
PubMed
Summary
This summary is machine-generated.

Researchers stabilized a disease-related protein variant (AR) implicated in light chain amyloidosis by introducing specific mutations. This work enhances understanding of protein stability and aggregation, crucial for developing new therapies.

Keywords:
AL amyloidosiscrystallographyfibrillogenesisthermodynamic analysis

More Related Videos

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

12.3K
Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by &#947;-Secretase
11:57

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

615

Related Experiment Videos

Last Updated: Feb 23, 2026

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood
13:14

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

11.0K
Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

12.3K
Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by &#947;-Secretase
11:57

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

615

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Light chain amyloidosis is a fatal condition caused by the aggregation of monoclonal immunoglobulin light chains, damaging organs.
  • The λ6a germ-line gene segment encodes a light chain implicated in this disease.
  • A patient-derived variant, AR, exhibits low stability and rapid in vitro fibril formation.

Purpose of the Study:

  • To enhance the thermodynamic stability of the AR variant by reverting specific residues to their germ-line sequence.
  • To investigate the structural basis for stabilization and destabilization effects of mutations.
  • To explore the assembly patterns of light chain variants.

Main Methods:

  • Site-directed mutagenesis to create AR-F21I, AR-F21/IV104L, and 6a-R25G variants.
  • Protein crystallization and X-ray crystallography to determine atomic structures.
  • Analysis of structural data to understand mutation effects and assembly.

Main Results:

  • The single mutant AR-F21I and double mutant AR-F21/IV104L showed significant stabilization, with mutations located in the hydrophobic core.
  • Mutation Arg25Gly in 6aJL2 destabilized the domain, while the reverse mutation in AR did not stabilize it as anticipated.
  • Crystallographic analysis revealed an octameric assembly in 6a-R25G, which was also observed in other variants, suggesting a common assembly pattern.

Conclusions:

  • Targeted mutations in the hydrophobic core can significantly stabilize disease-associated protein variants like AR.
  • Structural insights explain the differential effects of mutations on protein stability.
  • A conserved octameric assembly pattern exists across different light chain variants, providing a basis for understanding aggregation.