Rational design of amphiphilic fluorinated peptides : evaluation of self-assembly properties and hydrogel formation
| Autor: | Suvrat Chowdhary, Robert Franz Schmidt, Anil Kumar Sahoo, Tiemo tom Dieck, Thomas Hohmann, Boris Schade, Kerstin Brademann-Jock, Andreas F. Thünemann, Roland R. Netz, Michael Gradzielski, Beate Koksch |
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| Přispěvatelé: | Chemistry, Royal |
| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: |
amphiphilic fluorinated peptides
self-assembly properties ddc:540 Hydrogels General Materials Science Fluorine Peptides hydrogel formation 500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften Hydrophobic and Hydrophilic Interactions Protein Structure Secondary |
| Zdroj: | Nanoscale ChemRxiv : the Preprint Server for Chemistry |
| Popis: | 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, 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. |
| Databáze: | OpenAIRE |
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