Controlling the Helix Handedness of ααβ‐Peptide Foldamers through Sequence Shifting

Abstract

Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under http://dx.

The application of the hierarchical approach for the construction of foldameric peptide self-assembled nanostructures

“…24 In most of the studied cases, the introduction of the trans-b residue in the chosen positions of the coiled-coil structure did not change the location of the minima compared to the model peptides but influenced the R(y 222 /y 208 ) and mean residue ellipticity values, which is typical for helical a,b-peptides. 25 However, in the CD spectra of 1_c and 2_c, shifts of the minimum position from 208 to 211 and 206 nm, respectively, can be observed. Therefore, we can conclude that peptide 1_c possesses only a partially folded conformation with a high contribution from b-sheet structure, since the described peptide was only partially folded, showed a low Cotton effect, and was very prone to aggregation under the study conditions.…”

Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein–human ACE2 interaction

“…The ability of a peptide foldamer to form a helix can be indicated by the method of stereochemical patterning: a helical structure is formed if the appropriate ψ and ϕ dihedral angles flanking the amide bond are of the same sign 18 . It was demonstrated that α,β-peptides containing the backbone patterns ααβ, αααβ, and ααβαααβ can adopt helical conformations 16 , 19 , 20 . Peptide foldamers have had numerous successful applications in medicinal chemistry 21–26 .…”

Chemodiscrimination of Olefin Bonds Through Cross‐Metathesis Reactions – Synthesis of Functionalized β‐Lactam and β‐Amino Acid Derivatives

“…It is known that the new‐generation peptides built from β‐amino acid monomers are stable to both metabolism and proteases as well as peptidases. Consequently, they are regarded as valuable biomolecules for drug design …”