Zitieren Sie bitte immer diesen URN: urn:nbn:de:kobv:b43-553504
Rational design of amphiphilic fluorinated peptides: evaluation of self-assembly properties and hydrogel formation
- Advanced peptide-based nanomaterials composed of self-assembling peptides (SAPs) are of emerging interest in pharmaceutical and biomedical applications. The introduction of fluorine into peptides, in fact, offers unique opportunities to tune their biophysical properties and intermolecular interactions. In particular, the degree of fluorination plays a crucial role in peptide engineering as it can be used to control the characteristics of fluorine-specific interactions and, thus, peptide conformation and self-assembly. Here, we designed and explored a series of amphipathic peptides by incorporating the fluorinated amino acids (2S)-4-monofluoroethylglycine (MfeGly), (2S)-4,4-difluoroethylglycine (DfeGly) and (2S)-4,4,4-trifluoroethylglycine (TfeGly) as hydrophobic components. This approach enabled studying the impact of fluorination on secondary structure formation and peptide self-assembly on a systematic basis. We show that the interplay between polarity and hydrophobicity, bothAdvanced peptide-based nanomaterials composed of self-assembling peptides (SAPs) are of emerging interest in pharmaceutical and biomedical applications. The introduction of fluorine into peptides, in fact, offers unique opportunities to tune their biophysical properties and intermolecular interactions. In particular, the degree of fluorination plays a crucial role in peptide engineering as it can be used to control the characteristics of fluorine-specific interactions and, thus, peptide conformation and self-assembly. Here, we designed and explored a series of amphipathic peptides by incorporating the fluorinated amino acids (2S)-4-monofluoroethylglycine (MfeGly), (2S)-4,4-difluoroethylglycine (DfeGly) and (2S)-4,4,4-trifluoroethylglycine (TfeGly) as hydrophobic components. This approach enabled studying the impact of fluorination on secondary structure formation and peptide self-assembly on a systematic basis. We show that the interplay between polarity and hydrophobicity, both induced differentially by varying degrees of side chain fluorination, does affect peptide folding significantly. A greater degree of fluorination promotes peptide fibrillation and subsequent formation of physical hydrogels in physiological conditions. Molecular simulations revealed the key role played by electrostatically driven intra-chain and inter-chain contact pairs that are modulated by side chain fluorination and give insights into the different self-organization behaviour of selected peptides. Our study provides a systematic report about the distinct features of fluorinated oligomeric peptides with potential applications as peptide-based biomaterials.…
Autor*innen: | S. Chowdhary, R. F. Schmidt, A. K. Sahoo, T. tom Dieck, T. Hohmann, B. Schade, Kerstin Brademann-Jock, Andreas ThünemannORCiD, R. R. Netz, M. Gradzielski, B. Koksch |
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Dokumenttyp: | Zeitschriftenartikel |
Veröffentlichungsform: | Verlagsliteratur |
Sprache: | Englisch |
Titel des übergeordneten Werkes (Englisch): | Nanoscale |
Jahr der Erstveröffentlichung: | 2022 |
Organisationseinheit der BAM: | 6 Materialchemie |
6 Materialchemie / 6.5 Synthese und Streuverfahren nanostrukturierter Materialien | |
Veröffentlichende Institution: | Bundesanstalt für Materialforschung und -prüfung (BAM) |
Verlag: | Royal Society of Chemistry |
Jahrgang/Band: | 14 |
Ausgabe/Heft: | 28 |
Erste Seite: | 10176 |
Letzte Seite: | 10189 |
DDC-Klassifikation: | Technik, Medizin, angewandte Wissenschaften / Ingenieurwissenschaften / Ingenieurwissenschaften und zugeordnete Tätigkeiten |
Freie Schlagwörter: | Amyloid; SAXS; Small-angle X-ray scattering |
Themenfelder/Aktivitätsfelder der BAM: | Material |
Material / Nano | |
DOI: | 10.1039/D2NR01648F |
URN: | urn:nbn:de:kobv:b43-553504 |
ISSN: | 2040-3364 |
Verfügbarkeit des Dokuments: | Datei für die Öffentlichkeit verfügbar ("Open Access") |
Lizenz (Deutsch): | Creative Commons - CC BY - Namensnennung 4.0 International |
Datum der Freischaltung: | 25.07.2022 |
Referierte Publikation: | Ja |
Datum der Eintragung als referierte Publikation: | 25.07.2022 |
Schriftenreihen ohne Nummerierung: | Wissenschaftliche Artikel der BAM |