Rational design of amphiphilic fluorinated peptides: evaluation of self-assembly properties and hydrogel formation
Suvrat Chowdhary, Robert F. Schmidt, Anil Kumar Sahoo, Tiemo tom Dieck, Thomas Hohmann, Boris Schade, Kerstin Brademann-Jock, Andreas F. Thünemann, Roland R. Netz, Michael Gradzielski, Beate Koksch
Abstract
)-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.