# Investigation of the Aggregation of Aβ Peptide (1-40) in the Presence of κ-Carrageenan-Stabilised Liposomes Loaded with Homotaurine

## TL;DR

This study shows that homotaurine-loaded liposomes can inhibit the aggregation of Aβ peptides, which is linked to Alzheimer's disease.

## Contribution

The first use of particle size distribution analysis to study Aβ aggregation in the presence of homotaurine-loaded liposomes.

## Key findings

- Unloaded liposomes increased the size of 90% of particles in the dispersion.
- Homotaurine-loaded liposomes minimally affected larger particle sizes during aggregation.
- Homotaurine inhibits Aβ aggregation through charge effects and molecular crowding.

## Abstract

The kinetics of amyloid aggregation was studied indirectly by monitoring the changes in the polydispersity of mixed dispersion of amyloid β peptide (1-40) and composite liposomes. The liposomes were prepared from the 1,2-dioleoyl-sn-glicero-3-phoshocholine (DOPC) phospholipid and stabilised by the electrostatic adsorption of κ-carrageenan. The produced homotaurine-loaded and unloaded liposomes had a highly negative electrokinetic potential and remarkable stability in phosphate buffer (pH 4 and 7.4). For the first time, the appearance and evolution of the aggregation of Aβ were presented through the variation in the standard percentile readings (D10, D50, and D90) obtained from the particle size distribution analysis. The kinetic experiments indicated the appearance of the first aggregates almost 30 min after mixing the liposomes and peptide solution. It was observed that by adding unloaded liposomes, the size of 90% of the particles in the dispersion (D90) increased. In contrast, the addition of homotaurine-loaded liposomes had almost minimal impact on the size of the fractions of larger particles during the kinetic experiments. Despite the specific bioactivity of homotaurine in the presence of natural cell membranes, this study reported an additional inhibitory effect of the compound on the amyloid peptide aggregation due to the charge effects and ‘molecular crowding’.