Show simple item record

dc.contributor.authorVetri, Valeria
dc.contributor.authorPiccirilli, Federica
dc.contributor.authorKrausser, Johannes
dc.contributor.authorBuscarino, Gianpiero
dc.contributor.authorŁapińska, Urszula
dc.contributor.authorVestergaard, Bente
dc.contributor.authorZaccone, Alessio
dc.contributor.authorFoderà, Vito
dc.date.accessioned2018-05-18T13:55:33Z
dc.date.available2018-05-18T13:55:33Z
dc.date.issued2018-03-29
dc.identifier.issn1520-6106
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/275942
dc.description.abstractProtein self-assembly into amyloid fibrils or highly hierarchical superstructures is closely linked to neurodegenerative pathologies as Alzheimer's and Parkinson's diseases. Moreover, protein assemblies also emerged as building blocks for bioinspired nanostructured materials. In both the above mentioned fields, the main challenge is to control the growth and properties of the final protein structure. This relies on a more fundamental understanding of how interactions between proteins can determine structures and functions of biomolecular aggregates. Here, we identify a striking effect of the hydration of the single human insulin molecule and solvent properties in controlling hydrophobicity/hydrophilicity, structures, and morphologies of a superstructure named spherulite, observed in connection to Alzheimer's disease. Depending on the presence of ethanol, such structures can incorporate fluorescent molecules with different physicochemical features and span a range of mechanical properties and morphologies. A theoretical model providing a thorough comprehension of the experimental data is developed, highlighting a direct connection between the intimate physical protein-protein interactions, the growth, and the properties of the self-assembled superstructures. Our findings indicate structural variability as a general property for amyloid-like aggregates and not limited to fibrils. This knowledge is pivotal not only for developing effective strategies against pathological amyloids but also for providing a platform to design highly tunable biomaterials, alternative to elongated protein fibrils.
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherAmerican Chemical Society (ACS)
dc.subjectHumans
dc.subjectEthanol
dc.subjectAmyloid
dc.subjectMicroscopy, Confocal
dc.subjectMicroscopy, Electron, Transmission
dc.subjectMicroscopy, Atomic Force
dc.subjectNeutron Diffraction
dc.subjectSpectroscopy, Fourier Transform Infrared
dc.subjectCircular Dichroism
dc.subjectScattering, Small Angle
dc.subjectHydrophobic and Hydrophilic Interactions
dc.subjectInsulins
dc.subjectOptical Imaging
dc.titleEthanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid Spherulites.
dc.typeArticle
prism.endingPage3112
prism.issueIdentifier12
prism.publicationDate2018
prism.publicationNameJ Phys Chem B
prism.startingPage3101
prism.volume122
dc.identifier.doi10.17863/CAM.23223
dcterms.dateAccepted2018-03-01
rioxxterms.versionofrecord10.1021/acs.jpcb.8b01779
rioxxterms.versionAM
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2018-03-15
dc.contributor.orcidBuscarino, Gianpiero [0000-0001-8324-6783]
dc.contributor.orcidZaccone, Alessio [0000-0002-6673-7043]
dc.contributor.orcidFoderà, Vito [0000-0003-2855-0568]
dc.identifier.eissn1520-5207
rioxxterms.typeJournal Article/Review
cam.issuedOnline2018-03-15
rioxxterms.freetoread.startdate2019-02-28


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record