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Related Experiment Video

Updated: Jun 28, 2026

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

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Published on: July 13, 2013

Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan.

Lise Nesgaard¹, Brian Vad, Gunna Christiansen

¹Department of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.

Biochimica Et Biophysica Acta

|November 4, 2008

Summary

Familial Danish Dementia (FDD) involves the ADan peptide. This study shows SerADan peptide forms non-amyloid aggregates and permeabilizes membranes, revealing potential disease pathways.

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Last Updated: Jun 28, 2026

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

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Published on: July 13, 2013

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Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Familial Danish Dementia (FDD) is a neurodegenerative disease associated with the ADan peptide.
The cytotoxicity of ADan peptide is potentially linked to its interactions with cell membranes.

Purpose of the Study:

To characterize the aggregation and membrane interaction properties of SerADan, a modified ADan peptide.
To investigate the relationship between peptide aggregation, membrane permeabilization, and potential disease mechanisms in FDD.

Main Methods:

Peptide synthesis and characterization of SerADan.
Aggregation studies at various pH and ionic strengths.
Lipid vesicle binding and permeabilization assays.
Conformational analysis using spectroscopic methods.

Main Results:

SerADan rapidly forms beta-sheet rich fibril-like structures at pH 5.0 and 7.5, but these do not bind amyloid dyes.
Anionic lipid vesicles inhibit SerADan aggregation at neutral/acidic pH and low ionic strength.
Monomeric SerADan permeabilizes lipid vesicles by forming stable membrane-associated beta-sheet structures.
Solution aging of SerADan leads to reduced and eventually abolished membrane permeabilization.

Conclusions:

Non-fibrillar SerADan aggregates can form through a stepwise process, leading to diverse higher-order structures.
The balance between lipid binding and aggregation influences ADan peptide's in vivo pathway, potentially leading to inert aggregates or cytotoxic species.
Rapid formation of local beta-sheet structures may hinder progression to amyloid formation.