{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T02:02:33Z","timestamp":1790301753058,"version":"4.1.0"},"reference-count":61,"publisher":"American Chemical Society (ACS)","issue":"28","license":[{"start":{"date-parts":[[2018,6,20]],"date-time":"2018-06-20T00:00:00Z","timestamp":1529452800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology , Ministry of Science and Technology","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001409","name":"Department of Science and Technology, Ministry of Science and Technology","doi-asserted-by":"publisher","award":["SR\/NM\/NS-1143\/2016"],"award-info":[{"award-number":["SR\/NM\/NS-1143\/2016"]}],"id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,7,19]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Prevention and therapeutic strategies for various neurodegenerative diseases focus on inhibiting protein fibrillation, clearing aggregated protein plaques from the brain, and lowering protein-aggregate-induced toxicity. We have designed poly(trehalose) nanoparticles that can inhibit amyloid\/polyglutamine aggregation under extra-\/intracellular conditions, reduce such aggregation-derived cytotoxicity, and prevent polyglutamine aggregation in a Huntington\u2019s disease (HD) model mouse brain. The nanoparticles have a hydrodynamic size of 20\u201330 nm and are composed of a 6 nm iron oxide core and a zwitterionic polymer shell containing \u223c5\u201312 wt % covalently linked trehalose. The designed poly(trehalose) nanoparticles are 1000\u201310000 times more efficient than molecular trehalose in inhibiting protein fibrillation in extra-cellular space, in blocking aggregation of polyglutamine-containing mutant huntingtin protein in model neuronal cells, and in suppressing mutant huntingtin aggregates in HD mouse brain. We show that the nanoparticle form of trehalose with zwitterionic surface charge and a trehalose multivalency (i.e., number of trehalose molecules per nanoparticle) of \u223c80\u2013200 are crucial for efficient brain targeting, entry into neuronal cells, and suppression of mutant huntingtin aggregation. The present work shows that nanoscale trehalose can offer highly efficient antiamyloidogenic performance at micromolar concentration, compared with millimollar to molar concentrations for molecular trehalose. This approach can be extended to in vivo application to combat protein-aggregation-derived neurodegenerative diseases.<\/jats:p>","DOI":"10.1021\/acsami.7b06510","type":"journal-article","created":{"date-parts":[[2017,6,20]],"date-time":"2017-06-20T15:00:55Z","timestamp":1497970855000},"page":"24126-24139","source":"Crossref","is-referenced-by-count":147,"title":["Poly(trehalose)\nNanoparticles Prevent Amyloid Aggregation and Suppress Polyglutamine Aggregation in a Huntington\u2019s\nDisease Model Mouse"],"prefix":"10.1021","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4050-1187","authenticated-orcid":true,"given":"Koushik","family":"Debnath","sequence":"first","affiliation":[{"name":"Indian Association for the Cultivation of Science , , - ,","place":["Kolkata, India, 700032"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0303-5351","authenticated-orcid":true,"given":"Nibedita","family":"Pradhan","sequence":"additional","affiliation":[{"name":"Indian Association for the Cultivation of Science , , - ,","place":["Kolkata, India, 700032"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brijesh Kumar","family":"Singh","sequence":"additional","affiliation":[{"name":"National Brain Research Centre , , - ,","place":["Manesar, Gurgaon, India, 122051"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6549-4211","authenticated-orcid":true,"given":"Nihar R.","family":"Jana","sequence":"additional","affiliation":[{"name":"National Brain Research Centre , , - ,","place":["Manesar, Gurgaon, India, 122051"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4595-6917","authenticated-orcid":true,"given":"Nikhil R.","family":"Jana","sequence":"additional","affiliation":[{"name":"Indian Association for the Cultivation of Science , , - ,","place":["Kolkata, India, 700032"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2017,6,20]]},"reference":[{"key":"2026090315423289200_cit1","doi-asserted-by":"publisher","first-page":"A23","DOI":"10.1038\/399a023","article-title":"Translating\nCell Biology into Therapeutic Advances in Alzheimer\u2019s Disease","volume":"399","author":"Selkoe","year":"1999","journal-title":"Nature"},{"key":"2026090315423289200_cit2","doi-asserted-by":"publisher","first-page":"900","DOI":"10.1038\/nature02264","article-title":"Folding\nProteins in Fatal Ways","volume":"426","author":"Selkoe","year":"2003","journal-title":"Nature"},{"key":"2026090315423289200_cit3","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/S0891-0618(03)00029-2","article-title":"Recent Advances in\nUnderstanding the Pathogenesis of Polyglutamine Diseases: Involvement\nof Molecular Chaperones and Ubiquitin-Proteasome Pathway","volume":"26","author":"Jana","year":"2003","journal-title":"J. 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