Show simple item record

dc.contributor.authorErdogan, Hakan
dc.contributor.authorBabur, Esra
dc.contributor.authorYilmaz, Mehmet
dc.contributor.authorCandaş, Elif
dc.contributor.authorGordesel, Merve
dc.contributor.authorDede, Yavuz
dc.contributor.authorÖren, Ersin Emre
dc.contributor.authorDemirel, Gokcen Birlik
dc.contributor.authorOzturk, Mustafa Kemal
dc.contributor.authorYavuz, Mustafa Selman
dc.contributor.authorDemirel, Gokhan
dc.date.accessioned2019-05-23T05:48:45Z
dc.date.available2019-05-23T05:48:45Z
dc.date.issued2015-07
dc.identifier.citationErdogan, 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.issn0743-7463
dc.identifier.othernumber of pages 9
dc.identifier.urihttps://pubs.acs.org/doi/10.1021/acs.langmuir.5b01406
dc.identifier.urihttp://hdl.handle.net/20.500.11851/1034
dc.description.abstractSince 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.isoengen_US
dc.publisherAmer Chemical Socen_US
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectorganogelsen_US
dc.subjectnanotubesen_US
dc.subjectsolvatochromic comparison methoden_US
dc.subjectpeptideen_US
dc.subjectdensityen_US
dc.subjectsolventen_US
dc.subjectproteinsen_US
dc.subjectcrystalsen_US
dc.subjectsurfaceen_US
dc.subjectnanofibersen_US
dc.titleMorphological Versatility in the Self-Assembly of Val-Ala and Ala-Val Dipeptidesen_US
dc.typearticleen_US
dc.relation.journalLangmuiren_US
dc.contributor.departmentTOBB ETU, Faculty of Engineering, Department of Biomedical Engineeringen_US
dc.contributor.departmentTOBB ETÜ, Mühendislik Fakültesi, Biyomedikal Mühendisliği Bölümütr_TR
dc.identifier.volume31
dc.identifier.issue26
dc.identifier.startpage7337
dc.identifier.endpage7345
dc.relation.tubitakTUBITAK [111M237]en_US
dc.contributor.orcidhttps://orcid.org/0000-0001-5902-083X
dc.identifier.wosWOS:000357839200020
dc.identifier.scopus2-s2.0-84936817525
dc.contributor.tobbetuauthorÖren, Ersin Emre
dc.contributor.tobbetuauthorCandaş, Elif
dc.identifier.PubMedIDPMID:26086903
dc.identifier.doi10.1021/acs.langmuir.5b01406
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıtr_TR


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record