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SUMMARY:Special LMNN Seminar - Polymorphism of amyloid fibrils revealed by
  cryo electron microscopy
DTSTART:20180507T110000
DTEND:20180507T120000
DTSTAMP:20260916T034809Z
UID:5c82c477f9a6b1184baf18e755c01c645aab2eb8ce21769eec72941e
CATEGORIES:Conferences - Seminars
DESCRIPTION:Marcus Fändrich\, Institute of Protein Biochemistry\, Ulm Uni
 versity\, Ulm\, GERMANY\nPolymorphism describes the structural variations
  of amyloid fibrils formed by a given polypeptide chain. While there has b
 een long-standing evidence that structural variations of fibrils could und
 erlie different disease variants\, it remained controversial as to whether
  or not the fibrils within one patient or diseased animal are isomorphic. 
 Using improved methods to purify amyloid fibrils from diseased tissue and 
 electron microscopy we found that polymorphism is a conserved structural f
 eature of all analysed amyloid fibrils in vivo. That is\, irrespective of 
 whether we analysed diseased animals or patients\, amyloid deposits in dif
 ferent organs\, different amyloid precursor proteins and different forms o
 f amyloid diseases we uniformly found amyloid fibril polymorphism in one o
 rganism. Furthermore\, the same structural variations could be seen when a
 nalysing filaments from different tissues of the same patient. To obtain i
 nsights into the molecular basis of amyloid fibril polymorphism\, we used 
 cryo electron microscopy and applied it to fibrils formed from a peptide f
 ragment of an immunoglobulin light chain underlying systemic AL amyloidosi
 s. We find that the structure of experimentally observable fibril topologi
 es can be rationalized and predicted based on a small number of physical p
 arameters. Our data imply that a competition of molecular forces arising f
 rom β-sheet twist and cross-sectional interactions determines the formati
 on of the specific fibril architectures and their polymorphism in the expe
 rimental sample.
LOCATION:AI 1153 https://plan.epfl.ch/?room==AI%201153
STATUS:CONFIRMED
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