001035302 001__ 1035302
001035302 005__ 20250310131247.0
001035302 0247_ $$2doi$$a10.1016/j.jcis.2024.12.058
001035302 0247_ $$2ISSN$$a0021-9797
001035302 0247_ $$2ISSN$$a1095-7103
001035302 0247_ $$2datacite_doi$$a10.34734/FZJ-2025-00360
001035302 0247_ $$2pmid$$a39778472
001035302 0247_ $$2WOS$$aWOS:001407781400001
001035302 037__ $$aFZJ-2025-00360
001035302 082__ $$a540
001035302 1001_ $$00009-0005-9244-9538$$aLenton, Samuel$$b0
001035302 245__ $$aInsulin amyloid morphology is encoded in H-bonds and electrostatics interactions ruling protein phase separation
001035302 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2025
001035302 3367_ $$2DRIVER$$aarticle
001035302 3367_ $$2DataCite$$aOutput Types/Journal article
001035302 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1736434768_29027
001035302 3367_ $$2BibTeX$$aARTICLE
001035302 3367_ $$2ORCID$$aJOURNAL_ARTICLE
001035302 3367_ $$00$$2EndNote$$aJournal Article
001035302 520__ $$aIon-protein interactions regulate biological processes and are the basis of key strategies of modulating protein phase diagrams and stability in drug development. Here, we report the mechanisms by which H-bonds and electrostatic interactions in ion-protein systems determine phase separation and amyloid formation. Using microscopy, small-angle X-ray scattering, circular dichroism and atomistic molecular dynamics (MD) simulations, we found that anions specifically interacting with insulin induced phase separation by neutralising the protein charge and forming H-bond bridges between insulin molecules. The same interaction was responsible for an enhanced insulin conformational stability and resistance to oligomerisation. Under aggregation conditions, the anion-protein interaction translated into the activation of a coalescence process, leading to amyloid-like microparticles. This reaction is alternative to conformationally-driven pathways, giving rise to elongated amyloid-like fibrils and occurs in the absence of preferential ion-protein binding. Our findings depict a unifying scenario in which common interactions dictated both phase separation at low temperatures and the occurrence of pronounced heterogeneity in the amyloid morphology at high temperatures, similar to what has previously been reported for protein crystal growth.
001035302 536__ $$0G:(DE-HGF)POF4-5241$$a5241 - Molecular Information Processing in Cellular Systems (POF4-524)$$cPOF4-524$$fPOF IV$$x0
001035302 588__ $$aDataset connected to CrossRef, Journals: juser.fz-juelich.de
001035302 7001_ $$0P:(DE-HGF)0$$aChaaban, Hussein$$b1
001035302 7001_ $$0P:(DE-Juel1)180535$$aKhaled, Mohammed$$b2
001035302 7001_ $$00000-0002-8530-6441$$avan de Weert, Marco$$b3
001035302 7001_ $$0P:(DE-Juel1)132024$$aStrodel, Birgit$$b4$$eCorresponding author
001035302 7001_ $$00000-0003-2855-0568$$aFoderà, Vito$$b5$$eCorresponding author
001035302 773__ $$0PERI:(DE-600)1469021-4$$a10.1016/j.jcis.2024.12.058$$gVol. 683, p. 1175 - 1187$$p1175 - 1187$$tJournal of colloid and interface science$$v683$$x0021-9797$$y2025
001035302 8564_ $$uhttps://juser.fz-juelich.de/record/1035302/files/1-s2.0-S0021979724029102-main.pdf$$yOpenAccess
001035302 909CO $$ooai:juser.fz-juelich.de:1035302$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
001035302 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132024$$aForschungszentrum Jülich$$b4$$kFZJ
001035302 9131_ $$0G:(DE-HGF)POF4-524$$1G:(DE-HGF)POF4-520$$2G:(DE-HGF)POF4-500$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$9G:(DE-HGF)POF4-5241$$aDE-HGF$$bKey Technologies$$lNatural, Artificial and Cognitive Information Processing$$vMolecular and Cellular Information Processing$$x0
001035302 9141_ $$y2025
001035302 915__ $$0StatID:(DE-HGF)0160$$2StatID$$aDBCoverage$$bEssential Science Indicators$$d2023-10-21
001035302 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
001035302 915__ $$0StatID:(DE-HGF)0113$$2StatID$$aWoS$$bScience Citation Index Expanded$$d2023-10-21
001035302 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
001035302 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS$$d2024-12-20
001035302 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline$$d2024-12-20
001035302 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List$$d2024-12-20
001035302 915__ $$0StatID:(DE-HGF)1150$$2StatID$$aDBCoverage$$bCurrent Contents - Physical, Chemical and Earth Sciences$$d2024-12-20
001035302 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection$$d2024-12-20
001035302 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search$$d2024-12-20
001035302 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC$$d2024-12-20
001035302 920__ $$lyes
001035302 9201_ $$0I:(DE-Juel1)IBI-7-20200312$$kIBI-7$$lStrukturbiochemie$$x0
001035302 980__ $$ajournal
001035302 980__ $$aVDB
001035302 980__ $$aUNRESTRICTED
001035302 980__ $$aI:(DE-Juel1)IBI-7-20200312
001035302 9801_ $$aFullTexts