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Morphological Versatility in the Self-Assembly of Val-Ala and Ala-Val Dipeptides

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dc.contributor.author Erdogan, Hakan
dc.contributor.author Babur, Esra
dc.contributor.author Yilmaz, Mehmet
dc.contributor.author Candaş, Elif
dc.contributor.author Gordesel, Merve
dc.contributor.author Dede, Yavuz
dc.contributor.author Ören, Ersin Emre
dc.contributor.author Demirel, Gokcen Birlik
dc.contributor.author Ozturk, Mustafa Kemal
dc.contributor.author Yavuz, Mustafa Selman
dc.contributor.author Demirel, Gokhan
dc.date.accessioned 2019-05-23T05:48:45Z
dc.date.available 2019-05-23T05:48:45Z
dc.date.issued 2015-07
dc.identifier.citation Erdogan, H., Babur, E., Yilmaz, M., Candas, E., Gordesel, M., Dede, Y., ... & Demirel, G. (2015). Morphological versatility in the self-assembly of Val-Ala and Ala-Val dipeptides. Langmuir, 31(26), 7337-7345. en_US
dc.identifier.issn 0743-7463
dc.identifier.other number of pages 9
dc.identifier.uri https://pubs.acs.org/doi/10.1021/acs.langmuir.5b01406
dc.identifier.uri http://hdl.handle.net/20.500.11851/1034
dc.description.abstract Since the discovery of dipeptide self-assembly, diphenylalanine (Phe-Phe)-based dipeptides have been widely investigated in a variety of fields. Although various supramolecular Phe-Phe-based structures including tubes, vesicles, fibrils, sheets, necklaces, flakes, ribbons, and wires have been demonstrated by manipulating the external physical or chemical conditions applied, studies of the morphological diversity of dipeptides other than Phe-Phe are still required to understand both how these small molecules respond to external conditions such as the type of solvent and how the peptide sequence affects self-assembly and the corresponding molecular structures. In this work, we investigated the self-assembly of valine-alanine (Val-Ala) and alanine-valine (Ala-Val) dipeptides by varying the solvent medium. It was observed that Val-Ala dipeptide molecules may generate unique self-assembly-based morphologies in response to the solvent medium used. Interestingly, when Ala-Val dipeptides were utilized as a peptide source instead of Val-Ala, we observed distinct differences in the final dipeptide structures. We believe that such manipulation may not only provide us with a better understanding of the fundamentals of the dipeptide self-assembly process but also may enable us to generate novel peptide-based materials for various applications. en_US
dc.language.iso eng en_US
dc.publisher Amer Chemical Soc en_US
dc.rights info:eu-repo/semantics/closedAccess
dc.subject organogels en_US
dc.subject nanotubes en_US
dc.subject solvatochromic comparison method en_US
dc.subject peptide en_US
dc.subject density en_US
dc.subject solvent en_US
dc.subject proteins en_US
dc.subject crystals en_US
dc.subject surface en_US
dc.subject nanofibers en_US
dc.title Morphological Versatility in the Self-Assembly of Val-Ala and Ala-Val Dipeptides en_US
dc.type article en_US
dc.relation.journal Langmuir en_US
dc.contributor.department TOBB ETU, Faculty of Engineering, Department of Biomedical Engineering en_US
dc.contributor.department TOBB ETÜ, Mühendislik Fakültesi, Biyomedikal Mühendisliği Bölümü tr_TR
dc.identifier.volume 31
dc.identifier.issue 26
dc.identifier.startpage 7337
dc.identifier.endpage 7345
dc.relation.tubitak TUBITAK [111M237] en_US
dc.contributor.orcid Ören, Ersin Emre/0000-0001-5902-083X
dc.identifier.wos WOS:000357839200020
dc.identifier.scopus 2-s2.0-84936817525
dc.contributor.tobbetuauthor Ören, Ersin Emre
dc.contributor.tobbetuauthor Candaş, Elif
dc.contributor.YOKid Ören, Ersin Emre/21783
dc.identifier.PubMedID 26086903
dc.identifier.doi 10.1021/acs.langmuir.5b01406
dc.contributor.wosresearcherID Ören, Ersin Emre/B-5672-2011
dc.contributor.ScopusAuthorID Ören, Ersin Emre/35846321000
dc.contributor.ScopusAuthorID Candaş, Elif/56716306200
dc.relation.publicationcategory Uluslararası yayın tr_TR


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