N-methyl α-amino acids are important building elements of many naturally occurring antibiotics. Perfluoroarene-based peptide macrocycles: This stapling modification performed on a peptide sequence showed enhancement in binding, cell permeability, and proteolytic stability properties, as This method is selective towards cysteines and provides staples featuring lipophilic perfluorinated moieties. Perfluoroarene-Based peptide macrocycles contain rigid perfluoroaromatic staples. For example, the stitched peptide can be generated by the introduction of S5 at the i position, B5 at the i + 4 position, and S8 at the i + 11 position. The structure can increase α-helical content and protease resistance, enhance target binding affinity, and promote cell membrane penetration.Three types of stapled peptides are used with optimized combinations of non-natural building blocks such as (R)-N-Fmoc-2-(7'-octenyl) alanine and (S)-N-Fmoc-2-(4'-pentenyl) alanine. These peptides contain a synthetic brace, introduced across one face of an α-helix. Hydrocarbon stapled α-helical peptides are capable of targeting and interfering with intracellular protein-protein interactions. The hydrocarbon-stapling is achieved by ring-closing olefin metathesis between two functionalized non-natural building blocks, either R8-S5 or S5-S5. The stapled peptides can be used for intracellular drug targets because stapling can increase the target affinity and proteolytic resistance. LifeTein's stapling is carried out by covalently linking the side-chains of two amino acids, thereby forming a peptide macrocycle. Peptide stapling is a strategy for constraining short peptides in an alpha-helical conformation. These peptides are used to study protein interactions and post-translation modifications such as ubiquitination and phosphorylation. These 13C/15N peptides are similar to their native peptides in terms of chemical, physical properties, and biological activities. LifeTein offers stable isotope labeled peptides with amino acids enriched in 13C, and 15N. LifeTein offers stapled peptide synthesis and special amino acids and modifications, including Fluoromethylketone (FMK), Glycosylation, chloromethylketone (CMK), N-methyl amino acids, unnatural amino acids, acetyl-lysine, beta-alanine, aminobenzoic acid, amidation, acetylation, Abu, citrulline, Acm, dimethyl-lysine, hydroxy-proline (Hyp), methyl-lysine, mercaptopropionic acid, nitro-tyrosine, norleucine (Nle), pyro-glutamic acid (Pyr), carbobenzoxyl (Z), succinic acid, and sulfurylation. Modifications: Stapled peptide synthesis and special amino acids
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