Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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,...

Amyloid Fibrils

Amyloid Fibrils

Conformity

Conformity

Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.

Electron Affinity

Electron Affinity

The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).

Affinity and Avidity

Affinity and Avidity

Conformations of Butane

Conformations of Butane

Unlike ethane and propane that have only two major conformations, butane has more than two conformers. The staggered form of butane in which the bulky methyl groups on the two carbons are placed on opposite sides, that is, at a dihedral angle of 180°, is the lowest energy, most stable form — called the anti conformer. This conformation is stabilized due to the absence of steric repulsion between the largely spaced out methyl groups. The other two staggered conformations are...

You might also read

Related Articles

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

Sort by

Same author

Co-Delivery of Chemo and Immune Drugs by Prussian Blue Nanocubes for Combinational Therapy and <i>T</i><sub>1</sub>-<i>T</i><sub>2</sub>W MR Imaging of MDA-MB-231.

ACS applied bio materials·2026

Same author

The Role of Phase-Separated Condensates in Fusion Oncoprotein-Driven Cancers.

Annual review of cancer biology·2026

Same author

Protofibril Binding Peptides Recognize and Inhibit Huntingtin Amyloid Formation <i>in vitro</i> and <i>in vivo</i>.

bioRxiv : the preprint server for biology·2025

Same author

Contrary Effects of Cholesterol on Single-Component and Synaptic Vesicle Mimicking Lipid Bilayers.

The journal of physical chemistry letters·2025

Same author

KAT6A and KAT7 Histone Acetyltransferase Complexes Are Molecular Dependencies and Therapeutic Targets in NUP98-Rearranged Acute Myeloid Leukemia.

Cancer discovery·2025

Same author

Access, utilisation and barriers to lymphedema care: A mixed method study in Puducherry, India.

Acta tropica·2025

Search research articles

Related Experiment Video

Updated: Feb 12, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Aggregation-induced conformation changes dictate islet amyloid polypeptide (IAPP) membrane affinity.

Anoop Rawat¹, Barun Kumar Maity¹, Bappaditya Chandra¹

¹Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India.

Biochimica Et Biophysica Acta. Biomembranes

|April 8, 2018

Summary

Islet amyloid polypeptide (IAPP) aggregation, linked to Type II diabetes, shows toxic oligomers with higher membrane affinity due to conformational changes. This study reveals a distinct alpha-helical structure in toxic oligomers, enhancing their membrane binding.

Keywords:

Amyloid Raman Amyloid membrane interaction Conformational transition Fluorescence correlation spectroscopy Islet amyloid polypeptide Oligomer structure

More Related Videos

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

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

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

Published on: July 16, 2008

Related Experiment Videos

Last Updated: Feb 12, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

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

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

Published on: July 16, 2008

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Islet amyloid polypeptide (IAPP) is an intrinsically disordered protein implicated in Type II diabetes pathogenesis.
Amyloid aggregation, particularly of IAPP, involves oligomeric intermediates that are considered more cytotoxic than mature fibrils.
Cell membrane interaction is a critical factor in the toxicity of IAPP oligomers.

Purpose of the Study:

To investigate the relationship between the aggregation state of IAPP and its affinity for lipid membranes.
To characterize the conformational changes of IAPP during aggregation and their impact on membrane binding.
To elucidate the structural basis for the enhanced toxicity of IAPP oligomers.

Main Methods:

Forster Resonance Energy Transfer (FRET) to determine peptide conformation and end-to-end distance.
Spectroscopic techniques (Raman and Infrared) to analyze secondary structure content (alpha-helical vs. beta-sheet).
Binding assays using artificial lipid bilayers and RIN-m5F cell membranes to quantify peptide-membrane affinity.

Main Results:

IAPP affinity for artificial lipid bilayers was over 15 times higher for small oligomers (1.6 nm) compared to monomers (0.7 nm).
Qualitatively similar enhanced binding was observed with RIN-m5F cell membranes.
Monomeric IAPP exhibited a larger end-to-end distance than oligomeric forms, indicating a conformational transition.
Oligomers showed significant alpha-helical content, while larger aggregates were predominantly beta-sheet structures.

Conclusions:

The conformational change from monomer to alpha-helical oligomer significantly enhances IAPP's membrane affinity.
This altered conformation provides a structural basis for the increased toxicity of IAPP oligomers in Type II diabetes.
While conformational changes drive enhanced membrane affinity in toxic oligomers, the specific 'toxic fold' may not be universally conserved across all amyloidogenic peptides.