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dc.contributor.authorZengin, A.en_US
dc.contributor.authorCinar, G.en_US
dc.contributor.authorGuler, M. O.en_US
dc.date.accessioned2018-04-12T11:13:16Z
dc.date.available2018-04-12T11:13:16Z
dc.date.issued2017en_US
dc.identifier.issn1567-1739
dc.identifier.urihttp://hdl.handle.net/11693/37431
dc.description.abstractSupramolecular bioarchitectures formed by assembly of achiral or chiral building blocks play important roles in various biochemical processes. Stereochemistry of amino acids is important for structural organization of peptide and protein assemblies and structure-microenvironment interactions. In this study, oppositely charged peptide amphiphile (PA) molecules with L-, D- and mixture of L- and D-amino acid conformations are coassembled into supramolecular nanofibers and formed self-supporting gels at pH 7.4 in water. The enzymatic stability of the PA nanofiber gels was studied in the presence of proteinase K enzyme, which digest a broad spectrum of proteins and peptides. The structural changes on the chiral PA nanofibers were also analyzed at different time periods in the presence of enzymatic activity. Controlled release of a model cargo molecule through the chiral PA nanofiber gels was monitored. The diffusivity parameters were measured for all gel systems. Release characteristics and the enzymatic stability of the peptide nanofiber gels were modulated depending on organization of the chiral PA molecules within the supramolecular assemblies.en_US
dc.language.isoEnglishen_US
dc.source.titleCurrent Applied Physicsen_US
dc.relation.isversionofhttp://dx.doi.org/10.1016/j.cap.2017.02.026en_US
dc.subjectControlled releaseen_US
dc.subjectEnzymatic stabilityen_US
dc.subjectNanofibersen_US
dc.subjectPeptide amphiphileen_US
dc.subjectSelf-assemblyen_US
dc.subjectSupramolecular chiralityen_US
dc.subjectAmino acidsen_US
dc.subjectAmphiphilesen_US
dc.subjectEnzyme activityen_US
dc.subjectGelsen_US
dc.subjectMoleculesen_US
dc.subjectNanofibersen_US
dc.subjectPeptidesen_US
dc.subjectProteinsen_US
dc.subjectSelf assemblyen_US
dc.subjectStabilityen_US
dc.subjectSupramolecular chemistryen_US
dc.subjectChiral building blocksen_US
dc.subjectControlled releaseen_US
dc.subjectEnzymatic stabilityen_US
dc.subjectPeptide amphiphilesen_US
dc.subjectRelease characteristicsen_US
dc.subjectStructural organizationen_US
dc.subjectSupramolecular assembliesen_US
dc.subjectSupramolecular chiralityen_US
dc.subjectStereochemistryen_US
dc.titleControlled enzymatic stability and release characteristics of supramolecular chiral peptide amphiphile nanofiber gelsen_US
dc.typeArticleen_US
dc.departmentUNAM - Institute of Materials Science and Nanotechnology
dc.departmentNANOTAM - Nanotechnology Research Center
dc.citation.spage785en_US
dc.citation.epage792en_US
dc.citation.volumeNumber17en_US
dc.citation.issueNumber5en_US
dc.identifier.doi10.1016/j.cap.2017.02.026en_US
dc.publisherElsevier B.V.en_US
dc.embargo.release2019-05-01en_US
dc.identifier.eissn1878-1675en_US


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