Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.11851/1034
Title: Morphological Versatility in the Self-Assembly of Val-Ala and Ala-Val Dipeptides
Authors: Erdoğan, Hakan
Babur, Esra
Yılmaz, Mehmet
Candaş, Elif
Gordesel, Merve
Dede, Yavuz
Ören, Ersin Emre
Demirel, Gökçen Birlik
Öztürk, Mustafa Kemal
Yavuz, Mustafa Selman
Demirel, Gökhan
Keywords: organogels
nanotubes
solvatochromic comparison method
peptide
density
solvent
proteins
crystals
surface
nanofibers
Issue Date: Jul-2015
Publisher: Amer Chemical Soc
Source: 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.
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.
URI: https://pubs.acs.org/doi/10.1021/acs.langmuir.5b01406
https://hdl.handle.net/20.500.11851/1034
ISSN: 0743-7463
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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