Abstract:
Thepresynapticproteina-synuclein(aSyn)isan‘intrinsicallydisorderedprotein’thatishighlydynamicinconformation.TransientintramolecularinteractionsbetweenitschargedNandCtermini,andbetweenitshydrophobicregionandtheCterminus,preventself-association.Theseinteractionsinhibittheformationofinsolubleinclusions,whicharethepathologicalhallmarkofParkinson’sdiseaseandmanyothersynucleinopathies.ThisreviewdiscusseshowtheseintramolecularinteractionsareinfluencedbythespecificenvironmentaSynisin.Wediscusshowcharge,pH,calcium,andsaltaffectthephysiologicalstructureofmonomericaSyn,andhowtheymayfavourtheformationoftoxicstructures.ThemoreweunderstandthedynamicconformationsofaSyn,thebetterwecandesigndesperatelyneededtherapeuticstopreventdiseaseprogression.
Publication ID:
1041841
Published date:
7 December 2018 (Published online)
Publication source:
manual
Publication type:
Journal articles
Journal name:
Trends in Biochemical Sciences
Publication volume:
44
Publisher:
Elsevier
Parent title:
Edition:
Publication number: