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Observation of sequence specificity in the seeding of protein amyloid fibrils
Author(s) -
Krebs Mark R.H.,
MorozovaRoche Ludmilla A.,
Daniel Katie,
Robinson Carol V.,
Dobson Christopher M.
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04707004
Subject(s) - fibril , amyloid fibril , seeding , biophysics , lysozyme , amyloid (mycology) , chemistry , sequence (biology) , protein structure , protein aggregation , protein folding , crystallography , biochemistry , amyloid β , biology , disease , medicine , inorganic chemistry , pathology , agronomy
It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long‐range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease.