Company Filing History:
Years Active: 2020
Title: Discovering the Innovations of Daniel Frenzel
Introduction
Daniel Frenzel, an inventor based in Aachen, Germany, has made notable contributions to the field of biomedical research. His innovative approach to the quantitative characterization of substances has led to the development of a significant patent that aids in understanding amyloid-beta (Aβ) conformers.
Latest Patents
Frenzel holds a patent for a method aimed at quantitatively characterizing substances with respect to their properties of binding to amyloid-beta conformers. This invention involves several crucial steps: fractionating a sample containing various Aβ conformers, immobilizing a biotinylated Aβ conformer on a substrate that has a high affinity for biotin, and analyzing the binding behavior of a quality control probe against the Aβ conformer through measurement signals. This innovative method has implications for research in Alzheimer's disease and other amyloid-related conditions.
Career Highlights
Daniel Frenzel is affiliated with Forschungszentrum Jülich GmbH, where he applies his expertise in the realms of biochemistry and biophysics. His work primarily focuses on enzymology and molecular interactions, contributing to advancements in medical science through his innovative methods.
Collaborations
Throughout his career, Frenzel has collaborated with noted researchers such as Dieter Willbold and Julian Glueck. These collaborations have further enriched his research and have been pivotal in the success of his patent, enhancing the understanding of amyloid-related substances.
Conclusion
Daniel Frenzel's innovative contributions and patent in the characterization of amyloid-beta conformers are significant to the scientific community. His work not only showcases his capabilities as an inventor but also highlights the importance of interdisciplinary collaboration in driving scientific advancements. As research continues, Frenzel's methods promise to play a crucial role in developing therapies for diseases influenced by amyloid proteins.