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Macromol. Biosci. 3/2009
Author(s) -
Rekas Agata,
Lo Victor,
Gadd Gerry E.,
Cappai Roberto,
Yun Seok I.
Publication year - 2009
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200990004
Subject(s) - fibril , amyloid fibril , dendrimer , biophysics , amyloid (mycology) , chemistry , cover (algebra) , stereochemistry , amyloid β , biochemistry , biology , disease , medicine , inorganic chemistry , mechanical engineering , engineering
Back Cover: Dendrimer PAMAM interferes with amyloid pathway of α‐synuclein in two ways: it inhibits fibrillation in early stages and dissociates existing fibrils. The redirection of the protein by dendrimers from pathological forms to non‐toxic aggregates or preservation of native conformation, and especially their ability to dissociate existing fibrils offer therapeutic outlook for Parkinson's disease. Further details can be found in the article by A. Rekas, V. Lo, G. E. Gadd, R. Cappai, S. I. Yun on page 230.