N-Fmoc-N-methyl-(S)-2-allylglycine introduces N-methylation and an allyl substituent that reduce backbone flexibility and enable bioorthogonal derivatization. Researchers employ it to design sterically constrained peptides and reactive handles. The residue influences helix formation and hydrophobic interactions. Its protection ensures compatibility with multistep synthesis.
CAT No: R2174
CAS No:2606012-88-6
Synonyms/Alias:N-Fmoc-N-methyl-(S)-2-allylglycine;2606012-88-6;(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)(methyl)amino)pent-4-enoic acid;(2S)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl](methyl)amino}pent-4-enoic acid;SCHEMBL24633907;G87274;(2S)-2-[9H-fluoren-9-ylmethoxycarbonyl(methyl)amino]pent-4-enoic acid;
N-Fmoc-N-methyl-(S)-2-allylglycine is a structurally distinct amino acid derivative characterized by the presence of an N-terminal fluorenylmethyloxycarbonyl (Fmoc) protecting group, N-methylation, and an (S)-configured 2-allylglycine backbone. As an α-amino acid analog, it combines the conformational constraints and reactivity of the allyl side chain with the steric and electronic effects conferred by N-methylation. The Fmoc group facilitates compatibility with standard Fmoc solid-phase peptide synthesis (SPPS) protocols, making this compound particularly valuable for advanced peptide engineering. Its unique structure enables the exploration of peptide backbone modifications, conformational studies, and the design of novel peptidomimetics, supporting a wide range of research applications in chemical biology and synthetic peptide chemistry.
Peptide Synthesis: N-Fmoc-N-methyl-(S)-2-allylglycine serves as a versatile building block in Fmoc-based SPPS, enabling the incorporation of N-methylated and allyl-functionalized residues into custom peptide sequences. The Fmoc protection ensures orthogonality with other protecting groups, allowing for efficient chain elongation and selective deprotection steps. Incorporation of this amino acid analog into peptides can impart unique conformational features, such as increased rigidity or altered hydrogen-bonding patterns, which are valuable for probing structure-activity relationships and enhancing the metabolic stability of synthetic peptides.
Peptidomimetic Design: The presence of both N-methylation and an allyl side chain in this amino acid derivative provides an effective tool for the development of peptidomimetics with tailored structural and functional properties. N-methylation disrupts conventional backbone hydrogen bonding, promoting the adoption of noncanonical secondary structures and increasing resistance to enzymatic degradation. Meanwhile, the allyl group offers a chemically addressable handle for further functionalization or cross-linking, supporting the creation of conformationally constrained scaffolds and bioactive peptide analogs for structure-based drug design and molecular recognition studies.
Conformational Analysis: Researchers utilize N-Fmoc-N-methyl-(S)-2-allylglycine to investigate the impact of N-methylation and side-chain modifications on peptide folding, dynamics, and stability. By incorporating this residue into model peptides, it is possible to systematically assess how backbone methylation and the steric influence of the allyl group affect secondary structure formation, such as α-helix or β-turn propensity. These studies provide valuable insights into the fundamental principles governing peptide conformation, guiding the rational design of peptides with desired structural and functional attributes.
Chemical Ligation and Post-Synthetic Modification: The allyl functionality of this amino acid analog is amenable to a variety of chemoselective transformations, including cross-metathesis, allylation, and palladium-catalyzed deprotection reactions. These chemical handles enable site-specific post-synthetic modification of peptides, facilitating the introduction of fluorescent labels, affinity tags, or other bioorthogonal groups. Such modifications expand the utility of synthetic peptides in biochemical assays, molecular imaging, and target identification experiments.
Protease Resistance Studies: Incorporation of N-methylated residues, such as N-Fmoc-N-methyl-(S)-2-allylglycine, into peptide sequences is a well-established strategy for enhancing resistance to proteolytic cleavage. By systematically substituting native amino acids with N-methylated analogs, researchers can evaluate the effects on peptide stability in the presence of various proteases. These studies are instrumental for developing peptide-based probes and molecular tools with improved in vitro and in vivo stability, supporting applications in chemical biology, diagnostics, and therapeutic research.
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