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Macromolecular crowding can be mimicked in vitro by the addition of non-specific polymers, e.g. Ficoll, dextran and polyvinyl pyrrolidone (PVP), the latter being rarely used to study amyloid systems. We investigated the effect of PVP on amyloidogenesis of full-length human islet amyloid polypeptide (involved in type II diabetes) using fibrillisation and surface activity assays, ELISA, immunoblot and microscale thermophoresis. We demonstrate that high molecular mass PVP360 promotes amyloidogenesis due to volume exclusion and increase in effective amyloidogenic monomer concentration, like other crowders, but without the confounding effects of viscosity and surface activity. Interestingly, we also show that low molecular mass PVP10 has unique inhibitory properties as inhibition of fibril elongation occurs mainly in the bulk solution and is due to PVP10 directly and strongly interacting with amyloid species rather than the increase in viscosity typically associated with macromolecular crowding. In vivo, amyloidogenesis might be affected by the properties and proximity of endogenous macromolecular crowders, which could contribute to changes in associated pathogenesis. More generally, the PVP10 molecular backbone could be used to design small compounds as potential inhibitors of toxic species formation.<\/jats:p>","DOI":"10.1042\/bcj20180715","type":"journal-article","created":{"date-parts":[[2018,10,4]],"date-time":"2018-10-04T20:59:28Z","timestamp":1538686768000},"page":"3417-3436","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Multiphasic effect of vinyl pyrrolidone polymers on amyloidogenesis, from macromolecular crowding to inhibition"],"prefix":"10.1042","volume":"475","author":[{"given":"Richard","family":"Berwick","sequence":"first","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4901-9795","authenticated-orcid":false,"given":"David J.","family":"Vaux","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00e9titia","family":"Jean","sequence":"additional","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2018,11,9]]},"reference":[{"key":"2021112217001422000_BCJ-2018-0715C1","doi-asserted-by":"publisher","first-page":"678","DOI":"10.1007\/s00109-003-0464-5","article-title":"Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution","volume":"81","author":"Stefani","year":"2003","journal-title":"J. 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