Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.11851/1784
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dc.contributor.authorÇetinel, Sibel-
dc.contributor.authorDinçer, Sevil-
dc.contributor.authorCebeci, Anıl-
dc.contributor.authorÖren, Ersin Emre-
dc.contributor.authorWhitaker, John D.-
dc.contributor.authorSchwartz, Daniel T.-
dc.contributor.authorKaragüler, Nevin Gül-
dc.contributor.authorSarıkaya, Mehmet-
dc.contributor.authorTamerler, Candan-
dc.date.accessioned2019-07-08T13:29:34Z
dc.date.available2019-07-08T13:29:34Z
dc.date.issued2012
dc.identifier.citationCetinel, S., Dincer, S., Cebeci, A., Oren, E. E., Whitaker, J. D., Schwartz, D. T., ... & Tamerler, C. (2012). Peptides to bridge biological-platinum materials interface. Bioinspired, Biomimetic and Nanobiomaterials, 1(3), 143-153.en_US
dc.identifier.issn2045-9858
dc.identifier.urihttps://doi.org/10.1680/bbn.12.00008-
dc.identifier.urihttps://hdl.handle.net/20.500.11851/1784-
dc.description.abstractPeptides with inorganic materials recognition already started to impact a wide range of surface- related technologies ranging from biomonitoring to biomedical areas. Combinatorial biology- based libraries are the initial step in tempting the directed evolution of peptides with specifi c interactions towards technologically relevant materials. Here, a case study is provided to demonstrate the specifi c peptide binding and the amino acids residues that play an important role for platinum surface affi nity by combining computational as well as genetic engineering tools. Using a phage display technique, septapeptides were identifi ed exhibiting affi nity to noble metal platinum, and the amino acid distributions in the identifi ed peptides were analyzed. The analysis of the peptide sequences showed that strong Pt- binding peptides contain positively charged, hydrophilic, and polar residues, and especially enriched in threonine, serine, and glutamine. Under competitive surface- binding conditions, strong Pt- binding peptide motif displayed on phage resulted in high specifi city to Pt regions on a Pt- macropatterned glass. Conformational analysis of the strong binder indicates that threonine and serine as well as glutamine are in close contact with the surfaces forming a tripod molecular architecture. The alanine substitution mutagenesis applied at the genomic level to the peptide displayed on the phage revealed threonine and serine substitutions as the critical ones. Understanding the residue- based interactions of the peptide sequences can be utilized to tune the affi nity and the specifi city of the peptides with the inorganic surfaces, toward making them indispensable molecular tools to control the molecular interactions of biological macromolecules with the material surfaces.en_US
dc.language.isoenen_US
dc.publisherIce Publishingen_US
dc.relation.ispartofBioinspired Biomimetic And Nanobiomaterialsen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectplatinum binding peptidesen_US
dc.subjectbiointerfacesen_US
dc.subjectnanobiotechnologyen_US
dc.titlePeptides to bridge biological-platinum materials interfaceen_US
dc.typeArticleen_US
dc.departmentFaculties, Faculty of Engineering, Department of Biomedical Engineeringen_US
dc.departmentFakülteler, Mühendislik Fakültesi, Biyomedikal Mühendisliği Bölümütr_TR
dc.identifier.volume1
dc.identifier.issue3
dc.identifier.startpage143
dc.identifier.endpage153
dc.relation.tubitakTUBITAK/NSF-IRES Joint Project [107T250]en_US
dc.authorid0000-0001-5902-083X-
dc.identifier.wosWOS:000208935100002en_US
dc.identifier.scopus2-s2.0-84881078041en_US
dc.institutionauthorÖren, Ersin Emre-
dc.identifier.doi10.1680/bbn.12.00008-
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.relation.otherTurkish State Planning Organization (DPT) through The Advanced Technologies Program at Istanbul Technical Universityen_US
dc.relation.internationalUS Army Research Office through the DURINT Program (Defense University Research Initiative on NanoTechnology [DAAD19-01-1-0499]en_US
dc.relation.internationalNational Science Foundation through the Genetically Engineered Materials Science & Engineering Center (GEMSEC) at UW [DMR-0520567]en_US
dc.identifier.scopusqualityQ2-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.languageiso639-1en-
crisitem.author.dept02.2. Department of Biomedical Engineering-
Appears in Collections:Biyomedikal Mühendisliği Bölümü / Department of Biomedical Engineering
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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