Conexiant
Login
  • The Analytical Scientist
  • The Cannabis Scientist
  • The Medicine Maker
  • The Ophthalmologist
  • The Pathologist
  • The Traditional Scientist
The Analytical Scientist
  • Explore

    Explore

    • Latest
    • News & Research
    • Trends & Challenges
    • Keynote Interviews
    • Opinion & Personal Narratives
    • Product Profiles
    • App Notes

    Featured Topics

    • Mass Spectrometry
    • Chromatography
    • Spectroscopy

    Issues

    • Latest Issue
    • Archive
  • Topics

    Techniques & Tools

    • Mass Spectrometry
    • Chromatography
    • Spectroscopy
    • Microscopy
    • Sensors
    • Data and AI

    • View All Topics

    Applications & Fields

    • Clinical
    • Environmental
    • Food, Beverage & Agriculture
    • Pharma and Biopharma
    • Omics
    • Forensics
  • People & Profiles

    People & Profiles

    • Power List
    • Voices in the Community
    • Sitting Down With
    • Authors & Contributors
  • Business & Education

    Business & Education

    • Innovation
    • Business & Entrepreneurship
    • Career Pathways
  • Events
    • Live Events
    • Webinars
  • Multimedia
    • Video
Subscribe
Subscribe

False

The Analytical Scientist / App Notes / 2020 / Method Development for Analysis of Amyloid Beta Proteins

Method Development for Analysis of Amyloid Beta Proteins

01/24/2020

Share

Featured Image

Amyloid β (Aβ) are peptides of 36–43 amino acids that are derived from the amyloid precursor protein (APP) by cleavage with β- and γ- secretase. Aβ are the main components of amyloid plaques and therefore crucially involved in Alzheimer’s disease. The biological function of Aβ is still unexplained, but they are claimed to be neurotoxic as they form extracellular deposits in the brain and so can harm the cellular membrane.

To understand the function of the Aβ and for the research of Alzheimer’s disease, it is important to develop a reliable analysis for Aβ. However, this is not trivial as the Aβ peptides such as Aβ (1–42) are highly hydrophobic which leads to the formation of aggregates.

A method for the simultaneous determination of four Amyloid β using YMC-Triart Bio C4 has been developed by YMC. As the hydrophobic Aβ have the tendency to form aggregates a stationary phase with lower hydrophobicity and larger pore is needed, therefore YMC-Triart Bio C4 was chosen.

>> Download the full Application Note as PDF

Newsletters

Receive the latest analytical scientist news, personalities, education, and career development – weekly to your inbox.

Newsletter Signup Image

Explore More in Analytical Science

Dive deeper into the analytical science. Explore the latest articles, case studies, expert insights, and groundbreaking research.

False

Advertisement

Recommended

False

Related Content

Detection of residual pesticides on fruits and vegetables using Portability™ miniature mass spectrometer
Detection of residual pesticides on fruits and vegetables using Portability™ miniature mass spectrometer

June 9, 2020

Mass spectrometry can be now deployed for onsite pesticide screening in real time...

Routine monitoring of airborne VOCs using TD–GC×GC–TOF MS/FID
Routine monitoring of airborne VOCs using TD–GC×GC–TOF MS/FID

January 15, 2020

The identification and quantitation of volatile organic pollutants in air can be challenging, largely because of the complexity of the samples...

Quantifying trace odorants in water by GC–MS with trap-based preconcentration
Quantifying trace odorants in water by GC–MS with trap-based preconcentration

January 20, 2020

Assessing SPME and high‑capacity sorptive extracti...

Using Self-Aware Agilent InfinityLab LC/MSD iQ to Measure Trace-Level Impurities in a Brand Versus Generic Medication
Using Self-Aware Agilent InfinityLab LC/MSD iQ to Measure Trace-Level Impurities in a Brand Versus Generic Medication

January 22, 2020

This study presents a method for comparison of related impurities in a brand and a generic over-the-counter (OTC) acetaminophen drug...

False

The Analytical Scientist
Subscribe

About

  • About Us
  • Work at Conexiant Europe
  • Terms and Conditions
  • Privacy Policy
  • Advertise With Us
  • Contact Us

Copyright © 2025 Texere Publishing Limited (trading as Conexiant), with registered number 08113419 whose registered office is at Booths No. 1, Booths Park, Chelford Road, Knutsford, England, WA16 8GS.