Synthesis and self-assembly study of hybrid peptide foldamers for the development of functional supramolecular architectures

Abstract

Foldamers are conformationally three dimensional well - organized synthetic oligomers stabilized through non - covalent interactions. Hybrid peptide foldamers are amalgamated peptide sequences of natural and unnatural amino acids. Study of peptidic foldamers h elps to discover and fabricate novel peptide secondary structures through self - assembly with distinct functional properties. The presence of unnatural residues in hybrid foldamers could lead to significant proteolytic stability, structural versatility, bio compatibility and chemical robustness of peptide backbone and their self - assembled architectures. On the other hand, hybrid peptides containing  and  residues also expand the scope for the derivatization and to achieve a fine tuning of supramolecular mat erial properties. Thus, it is promising to solve and explore the structural, self - assembling and functional properties of hybrid peptides. The folded conformations and self - assembling architectures of hybrid peptides can be developed with potential applica tions in biomedical and material sciences.