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dc.contributor.authorHerling, Thereseen
dc.contributor.authorLevin, Aviaden
dc.contributor.authorSaar, Kadien
dc.contributor.authorDobson, Christopheren
dc.contributor.authorKnowles, Tuomasen
dc.date.accessioned2018-05-03T14:30:59Z
dc.date.available2018-05-03T14:30:59Z
dc.date.issued2018-03en
dc.identifier.issn1473-0197
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/275528
dc.description.abstractThe self-assembly of proteins into supra-molecular structures and machinery underpins biologi- cal activity in living systems. Misassembled, misfolded and aggregated protein structures can, by contrast, have deleterious activity and such species are at the origin of a number of disease states ranging from cancer to neurodegenerative disorders. In particular, the formation of highly ordered protein aggregates, amyloid fibrils, from normally soluble peptides and proteins, is the common pathological hallmark of a range a group of over fifty protein misfolding disorders. Because of the critical role of the process in the aetiology of such disorders, as well as the quest to understand the basic principles of protein folding and misfolding, the amyloid phenomenon has become a central area of modern biomedical research. Advances in our knowledge of the physical prop- erties of amyloid systems have, however, also highlighted the potential of amyloid structures in the context of materials science. In this review, we explore how microfluidic approaches can be used to study aspects of amyloid assembly and behaviour that are challenging to probe under bulk solution conditions. We discuss the use of volume confinement to probe very early events in the amyloid formation process. In addition, the well-defined fluid flow properties within chan- nels with dimensions on the micron scale can be exploited to measure the physical properties of protein aggregates, such as their sizes and charges, to shed light on the physical and chemical parameters defining amyloid species. Moreover, the molecular species formed during aggregation reactions have physical dimensions spanning at least three orders of magnitude, and microfluidic techniques are well suited to work with analytes of such disparate dimensions. Furthermore, the flexibility of the design of microfluidic devices lends itself to adaptable experimental setups, includ- ing the study of protein self-assembly within living cells. Finally, we highlight the salient features of microfluidic experiments that facilitate probing complex biological systems, and discuss their use in the exploration of amyloid as a class of functional material.
dc.format.mediumPrinten
dc.languageengen
dc.publisherRSC
dc.subjectHumansen
dc.subjectAmyloiden
dc.subjectMicrofluidic Analytical Techniquesen
dc.subjectProtein Conformationen
dc.subjectProtein Aggregatesen
dc.titleMicrofluidic approaches for probing amyloid assembly and behaviour.en
dc.typeArticle
prism.endingPage1016
prism.issueIdentifier7en
prism.publicationDate2018en
prism.publicationNameLab on a chipen
prism.startingPage999
prism.volume18en
dc.identifier.doi10.17863/CAM.22764
dcterms.dateAccepted2018-02-01en
rioxxterms.versionofrecord10.1039/c7lc01241aen
rioxxterms.versionAM*
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2018-03en
dc.contributor.orcidLevin, Aviad [0000-0002-3949-1033]
dc.contributor.orcidSaar, Kadi [0000-0002-5926-3628]
dc.contributor.orcidKnowles, Tuomas [0000-0002-7879-0140]
dc.identifier.eissn1473-0189
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idEuropean Research Council (337969)
pubs.funder-project-idEuropean Commission FP6 Specific Targeted Research Projects (STReP) (LSHM-CT-2006-037525)
pubs.funder-project-idBBSRC (1127850)
pubs.funder-project-idEPSRC (1510942)
pubs.funder-project-idBBSRC (BB/J002119/1)
rioxxterms.freetoread.startdate2019-03-12


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