Supramolecular nanostructure formation of coassembled amyloid inspired peptides

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buir.contributor.authorGüler, Mustafa O.
dc.citation.epage6514en_US
dc.citation.issueNumber25en_US
dc.citation.spage6506en_US
dc.citation.volumeNumber32en_US
dc.contributor.authorCinar, G.en_US
dc.contributor.authorOrujalipoor, I.en_US
dc.contributor.authorSu, C.-J.en_US
dc.contributor.authorJeng, U.-S.en_US
dc.contributor.authorIde, S.en_US
dc.contributor.authorGüler, Mustafa O.en_US
dc.date.accessioned2018-04-12T10:51:24Z
dc.date.available2018-04-12T10:51:24Z
dc.date.issued2016-06en_US
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)en_US
dc.description.abstractCharacterization of amyloid-like aggregates through converging approaches can yield deeper understanding of their complex self-assembly mechanisms and the nature of their strong mechanical stability, which may in turn contribute to the design of novel supramolecular peptide nanostructures as functional materials. In this study, we investigated the coassembly kinetics of oppositely charged short amyloid-inspired peptides (AIPs) into supramolecular nanostructures by using confocal fluorescence imaging of thioflavin T binding, turbidity assay and in situ small-angle X-ray scattering (SAXS) analysis. We showed that coassembly kinetics of the AIP nanostructures were consistent with nucleation-dependent amyloid-like aggregation, and aggregation behavior of the AIPs was affected by the initial monomer concentration and sonication. Moreover, SAXS analysis was performed to gain structural information on the size, shape, electron density, and internal organization of the coassembled AIP nanostructures. The scattering data of the coassembled AIP nanostructures were best fitted into to a combination of polydisperse core-shell cylinder (PCSC) and decoupling flexible cylinder (FCPR) models, and the structural parameters were estimated based on the fitting results of the scattering data. The stability of the coassembled AIP nanostructures in both fiber organization and bulk viscoelastic properties was also revealed via temperature-dependent SAXS analysis and oscillatory rheology measurements, respectively.en_US
dc.description.provenanceMade available in DSpace on 2018-04-12T10:51:24Z (GMT). No. of bitstreams: 1 bilkent-research-paper.pdf: 179475 bytes, checksum: ea0bedeb05ac9ccfb983c327e155f0c2 (MD5) Previous issue date: 2016en
dc.identifier.doi10.1021/acs.langmuir.6b00704en_US
dc.identifier.issn0743-7463
dc.identifier.urihttp://hdl.handle.net/11693/36734
dc.language.isoEnglishen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.isversionofhttps://doi.org/10.1021/acs.langmuir.6b00704en_US
dc.source.titleLangmuiren_US
dc.subjectCylinders (shapes)en_US
dc.subjectFunctional materialsen_US
dc.subjectGlycoproteinsen_US
dc.subjectMechanical stabilityen_US
dc.subjectNanostructuresen_US
dc.subjectPeptidesen_US
dc.subjectSelf assemblyen_US
dc.subjectSupramolecular chemistryen_US
dc.subjectViscoelasticityen_US
dc.subjectX ray scatteringen_US
dc.subjectAmyloid-like aggregatesen_US
dc.subjectConfocal fluorescence imagingen_US
dc.subjectMonomer concentrationen_US
dc.subjectOscillatory rheologiesen_US
dc.subjectStructural informationen_US
dc.subjectSupra-molecular nano structuresen_US
dc.subjectTemperature dependenten_US
dc.subjectViscoelastic propertiesen_US
dc.subjectProteinsen_US
dc.titleSupramolecular nanostructure formation of coassembled amyloid inspired peptidesen_US
dc.typeArticleen_US

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