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dc.contributor.authorÇınar, Göksuen_US
dc.contributor.authorCeylan, Hakanen_US
dc.contributor.authorUrel, Mustafaen_US
dc.contributor.authorErkal, Turan S.en_US
dc.contributor.authorTekin, E. Denizen_US
dc.contributor.authorTekinay, Ayse B.en_US
dc.contributor.authorDâna, Aykutluen_US
dc.contributor.authorGuler, Mustafa O.en_US
dc.date.accessioned2016-02-08T09:44:31Z
dc.date.available2016-02-08T09:44:31Z
dc.date.issued2012en_US
dc.identifier.issn1525-7797
dc.identifier.urihttp://hdl.handle.net/11693/21306
dc.description.abstractAmyloid peptides are important components in many degenerative diseases as well as in maintaining cellular metabolism. Their unique stable structure provides new insights in developing new materials. Designing bioinspired self-assembling peptides is essential to generate new forms of hierarchical nanostructures. Here we present oppositely charged amyloid inspired peptides (AIPs), which rapidly self-assemble into nanofibers at pH 7 upon mixing in water caused by noncovalent interactions. Mechanical properties of the gels formed by self-assembled AIP nanofibers were analyzed with oscillatory rheology. AIP gels exhibited strong mechanical characteristics superior to gels formed by self-assembly of previously reported synthetic short peptides. Rheological studies of gels composed of oppositely charged mixed AIP molecules (AIP-1 + 2) revealed superior mechanical stability compared to individual peptide networks (AIP-1 and AIP-2) formed by neutralization of net charges through pH change. Adhesion and elasticity properties of AIP mixed nanofibers and charge neutralized AIP-1, AIP-2 nanofibers were analyzed by high resolution force-distance mapping using atomic force microscopy (AFM). Nanomechanical characterization of self-assembled AIP-1 + 2, AIP-1, and AIP-2 nanofibers also confirmed macroscopic rheology results, and mechanical stability of AIP mixed nanofibers was higher compared to individual AIP-1 and AIP-2 nanofibers self-assembled at acidic and basic pH, respectively. Experimental results were supported with molecular dynamics simulations by considering potential noncovalent interactions between the amino acid residues and possible aggregate forms. In addition, HUVEC cells were cultured on AIP mixed nanofibers at pH 7 and biocompatibility and collagen mimetic scaffold properties of the nanofibrous system were observed. Encapsulation of a zwitterionic dye (rhodamine B) within AIP nanofiber network was accomplished at physiological conditions to demonstrate that this network can be utilized for inclusion of soluble factors as a scaffold for cell culture studies. © 2012 American Chemical Society.en_US
dc.language.isoEnglishen_US
dc.source.titleBiomacromoleculesen_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/bm301141hen_US
dc.titleAmyloid inspired self-assembled peptide nanofibersen_US
dc.typeArticleen_US
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)en_US
dc.departmentNanotechnology Research Center (NANOTAM)en_US
dc.departmentAysel Sabuncu Brain Research Center (BAM)en_US
dc.citation.spage3377en_US
dc.citation.epage3387en_US
dc.citation.volumeNumber13en_US
dc.citation.issueNumber10en_US
dc.identifier.doi10.1021/bm301141hen_US
dc.publisherAmerican Chemical Societyen_US
dc.contributor.bilkentauthorÇınar, Göksu
dc.contributor.bilkentauthorCeylan, Hakan
dc.contributor.bilkentauthorUrel, Mustafa
dc.contributor.bilkentauthorErkal, Turan S.
dc.contributor.bilkentauthorTekin, E. Deniz
dc.contributor.bilkentauthorTekinay, Ayse B.
dc.contributor.bilkentauthorDâna, Aykutlu
dc.contributor.bilkentauthorGuler, Mustafa O.
dc.identifier.eissn1526-4602


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