{Reference Type}: Journal Article
{Title}: Synthesis, derivatization, and conformational scanning of peptides containing N-Aminoglycine.
{Author}: Starnes SK;Del Valle JR;
{Journal}: Methods Enzymol
{Volume}: 698
{Issue}: 0
{Year}: 2024
{Factor}: 1.682
{DOI}: 10.1016/bs.mie.2024.04.018
{Abstract}: N-alkylated glycine residues are the main constituent of peptoids and peptoid-peptide hybrids that are employed across the biomedical and materials sciences. While the impact of backbone N-alkylation on peptide conformation has been extensively studied, less is known about the effect of N-amination on the secondary structure propensity of glycine. Here, we describe a convenient protocol for the incorporation of N-aminoglycine into host peptides on solid support. Amide-to-hydrazide substitution also affords a nucleophilic handle for further derivatization of the backbone. To demonstrate the utility of late-stage hydrazide modification, we synthesized and evaluated the stability of polyproline II helix and β-hairpin model systems harboring N-aminoglycine derivatives. The described procedures provide facile entry into peptidomimetic libraries for conformational scanning.