BEGIN:VCALENDAR VERSION:2.0 PRODID:-//DTU.dk//NONSGML DTU.dk//EN CALSCALE:GREGORIAN BEGIN:VEVENT DTSTART:20191122T143000Z DTEND:20191122T160000Z SUMMARY:Professortiltrædelse - Alexander Kai Büll DESCRIPTION:
Den 1. april 2019 blev Alexander Kai Büll udnævnt til professor på DTU Bioengineering.
\nDette fejres med en professortiltrædelsesforelæsning af Alexander Kai Büll med titlen:
\nBiomolecular self-assembly - from disease mechanisms to biomaterials
\nEfter forelæsningen vil der være en reception. Tilmelding er ikke nødvendig.
\nAbstract:
\nBiomolecular self-assembly - from disease mechanisms to biomaterials
\nThe self-assembly of biomolecules, in particular proteins, into ordered structures is a fascinating process that plays important roles in both biological function and disease. In this inaugural lecture I will highlight some of the contributions I have made to an increased understanding of the mechanisms of amyloid fibril formation, a process most notably linked to neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. I will also discuss how such mechanistic information can be used to characterize the mode of action of potential inhibitors of these processes.
\nAmyloid fibrils are not only formed by disease-related proteins, but also by proteins without any link to human disease, and which can be obtained in large quantities. I will present some studies that aim to exploit the self-assembly of such proteins, as well as synthetic peptides for the creation of biomaterials.
\nDen 1. april 2019 blev Alexander Kai Büll udnævnt til professor på DTU Bioengineering.
\nDette fejres med en professortiltrædelsesforelæsning af Alexander Kai Büll med titlen:
\nBiomolecular self-assembly - from disease mechanisms to biomaterials
\nEfter forelæsningen vil der være en reception. Tilmelding er ikke nødvendig.
\nAbstract:
\nBiomolecular self-assembly - from disease mechanisms to biomaterials
\nThe self-assembly of biomolecules, in particular proteins, into ordered structures is a fascinating process that plays important roles in both biological function and disease. In this inaugural lecture I will highlight some of the contributions I have made to an increased understanding of the mechanisms of amyloid fibril formation, a process most notably linked to neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. I will also discuss how such mechanistic information can be used to characterize the mode of action of potential inhibitors of these processes.
\nAmyloid fibrils are not only formed by disease-related proteins, but also by proteins without any link to human disease, and which can be obtained in large quantities. I will present some studies that aim to exploit the self-assembly of such proteins, as well as synthetic peptides for the creation of biomaterials.
\n