Welcome to the Fändrich Group
Our group is interested in studying the formation and properties of amyloid fibrils and related polypeptide aggregates. Amyloid fibrils can be
formed from many natural and non-natural polypeptide chains. Their formation is thought to represent a fundamental chemical property of
polypeptide chains as organic polymers. Inside the human body, amyloid states can occur associated with ageing and disease, such as in
Alzheimer's disease.
The various projects of our group aim to understand the molecular basis why and how polypeptide chains form amyloid aggregates.
Furthermore, we analyse possible biological and pathological effects of amyloid states and possiblities of interference. This work could lead to
new diagnostic procedures and may provide clues for novel therapeutic strategies. Our work relates to the research areas of biophysics,
structural biology, cell biology, neurobiology and biotechnology.
Selected reviews:
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Fändrich M
On the structural definition of amyloid fibrils and other polypeptide aggregates
Cellular and Molecular Life Sciences 2007, 64, 16/2007, 2066-2078
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Fändrich M, Meinhardt J, Grigorieff N
Structural polymorphism of Alzheimer Aß and other amyloid fibrils. (Review)
Prion 2009, 3, 89-93
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Fändrich M, Schmidt M, Grigorieff N
Review: Recent progress in understanding Alzheimer’s β-amyloid structures.
TiBS, 2011, 36, 338-345
● Morgado I, Fändrich M
Review: Assembly of Alzheimer's Aβ peptide into nanostructured amyloid fibrils.
Current Opinion in Colloid and Interface Science, 2011,16, 508-514
● Fändrich M
Review: Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity
J. Mol. Biol. 2012
Last Update:
01.03.2012
