Efficient synthesis and characterisation of the amyloid beta peptide, Aβ1-42, using a double linker system.

Iman Kavianinia,Paul W R Harris,Margaret A Brimble,Jin Ng,Nigel P Birch,Johanes K Kasim

doi:10.1039/c8ob02929f

Iman Kavianinia, Paul W R Harris + Show 4 more

Open Access

https://doi.org/10.1039/c8ob02929f

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Abstract

The amyloidogenic Aβ42 peptide was efficiently prepared using a double linker system, markedly improving solubility and chromatographic peak resolution, thus enabling full characterisation using standard techniques. The tag was readily cleaved with sodium hydroxide and removed by aqueous extraction, affording Aβ42 in high purity and yield for biophysical characterisation studies.

Highlights

The amyloidogenic Aβ42 peptide was efficiently prepared using a double linker system, markedly improving solubility and chromatographic peak resolution, enabling full characterisation using standard techniques
Endogenous Aβ peptide is derived from enzymatic processing of the transmembrane Amyloid Precursor Protein (APP) by the secretase family of enzymes
It is understood that in the disease state, there is a preferential shift towards the latter process, which results in the excessive production of Aβ peptide, leading to its gradual aggregation into plaques

Summary

Introduction

Efficient synthesis and characterisation of the amyloid beta peptide, Aβ1–42, using a double linker system† The amyloidogenic Aβ42 peptide was efficiently prepared using a double linker system, markedly improving solubility and chromatographic peak resolution, enabling full characterisation using standard techniques.

Results

Conclusion