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 Experiment Videos

Surface-catalyzed amyloid fibril formation.

Min Zhu1, Pierre O Souillac, Cristian Ionescu-Zanetti

  • 1Department of Chemistry and Biochemistry and the Department of Physics, University of California, Santa Cruz, California 95064, USA.

The Journal of Biological Chemistry
|October 3, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Photolysis of ortho-Nitrobenzyl Esters: Kinetics and Substituent Effects.

ACS omega·2025
Same author

Sensitivity, specificity, and accuracy of a liquid biopsy approach utilizing molecular amplification pools.

Scientific reports·2021
Same author

Detection of circulating tumour cells in patients with epithelial ovarian cancer by a microfluidic system.

International journal of clinical and experimental pathology·2020
Same author

ERASE-Seq: Leveraging replicate measurements to enhance ultralow frequency variant detection in NGS data.

PloS one·2018
Same author

Circulating Tumor Cells as Potential Biomarkers in Bladder Cancer.

The Journal of urology·2015
Same author

Biophysical Characterization of α-Synuclein and Rotenone Interaction.

Biomolecules·2014

Surface interactions accelerate light chain amyloidosis fibril formation. This study reveals novel fibril growth mechanisms on surfaces, offering insights into in vivo amyloid deposition in light chain amyloidosis.

Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Light chain (AL) amyloidosis involves pathological deposition of immunoglobulin light chain fragment fibrils.
  • These deposits occur in tissues, blood vessels, and basement membranes.

Purpose of the Study:

  • To investigate the in vitro assembly of a recombinant amyloidogenic light chain variable domain (SMA).
  • To monitor SMA fibril formation on various surfaces using atomic force microscopy.

Main Methods:

  • Utilized atomic force microscopy to observe SMA assembly on different surfaces.
  • Varied surface properties (charge, hydrophobicity) and pH conditions.

Main Results:

  • SMA formed fibrils on native mica at pH 5.0, unlike amorphous aggregates in solution.

Related Experiment Videos

  • Fibril formation was significantly faster and occurred at lower concentrations on surfaces.
  • Novel fibril growth mechanisms, including bidirectional assembly and growth from amorphous cores, were observed.
  • No fibrils formed on hydrophobic or positively charged surfaces, or at pH >7.0.

    • Conclusions:

    • Surfaces can significantly accelerate and alter the mechanism of SMA fibril formation compared to solution.
    • Observed surface-induced fibril growth may be more physiologically relevant to in vivo amyloidosis.
    • Understanding surface interactions is crucial for elucidating amyloidosis pathogenesis.