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To this end, we have engineered the\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b2<\/mml:mi>\n                    <\/mml:math>\n                    -wrapin AS69 to bind monomeric\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b1<\/mml:mi>\n                    <\/mml:math>\n                    -synuclein with high affinity. In cultured cells, AS69 reduced the self-interaction of\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b1<\/mml:mi>\n                    <\/mml:math>\n                    -synuclein and formation of visible\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b1<\/mml:mi>\n                    <\/mml:math>\n                    -synuclein aggregates. In flies, AS69 reduced\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b1<\/mml:mi>\n                    <\/mml:math>\n                    -synuclein aggregates and the locomotor deficit resulting from\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b1<\/mml:mi>\n                    <\/mml:math>\n                    -synuclein expression in neuronal cells. In biophysical experiments in vitro, AS69 highly sub-stoichiometrically inhibited both primary and autocatalytic secondary nucleation processes, even in the presence of a large excess of monomer. We present evidence that the AS69-\n                    <mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\">\n                      <mml:mi>\u03b1<\/mml:mi>\n                    <\/mml:math>\n                    -synuclein complex, rather than the free AS69, is the inhibitory species responsible for sub-stoichiometric inhibition of secondary nucleation. These results represent a new paradigm that high affinity monomer binders can lead to strongly sub-stoichiometric inhibition of nucleation processes.\n                  <\/jats:p>","DOI":"10.7554\/elife.46112","type":"journal-article","created":{"date-parts":[[2019,8,7]],"date-time":"2019-08-07T08:00:15Z","timestamp":1565164815000},"source":"Crossref","is-referenced-by-count":70,"title":["An engineered monomer binding-protein for \u03b1-synuclein efficiently inhibits the proliferation of amyloid fibrils"],"prefix":"10.7554","volume":"8","author":[{"given":"Emil Dandanell","family":"Agerschou","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Physikalische Biologie, Heinrich Heine University D\u00fcsseldorf, D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1204-5340","authenticated-orcid":true,"given":"Patrick","family":"Flagmeier","sequence":"additional","affiliation":[{"name":"Department of Chemistry, 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