The Cellular Environment Affects Monomeric α-Synuclein Structure
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Abstract
Thepresynapticproteina-synuclein(aSyn)isan‘intrinsicallydisorderedprotein’thatishighlydynamicinconformation.TransientintramolecularinteractionsbetweenitschargedNandCtermini,andbetweenitshydrophobicregionandtheCterminus,preventself-association.Theseinteractionsinhibittheformationofinsolubleinclusions,whicharethepathologicalhallmarkofParkinson’sdiseaseandmanyothersynucleinopathies.ThisreviewdiscusseshowtheseintramolecularinteractionsareinfluencedbythespecificenvironmentaSynisin.Wediscusshowcharge,pH,calcium,andsaltaffectthephysiologicalstructureofmonomericaSyn,andhowtheymayfavourtheformationoftoxicstructures.ThemoreweunderstandthedynamicconformationsofaSyn,thebetterwecandesigndesperatelyneededtherapeuticstopreventdiseaseprogression.
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Trends in Biochemical Sciences
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0167-7640
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44
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Elsevier
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