Fmoc-2-Me-Nle-OH is a methylated norleucine derivative offering enhanced steric bulk and modulated hydrophobicity. Researchers use it to study helix formation, packing density, and side-chain interactions. Its modified structure supports design of stabilized peptidomimetic frameworks.
CAT No: R2169
CAS No:2226710-38-7
Synonyms/Alias:Fmoc-2-Me-Nle-OH;2226710-38-7;Fmoc-a-methyl-L-norleucine;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-2-methylhexanoic acid;(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-2-methylhexanoic acid;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-2-methyl-hexanoic acid;(2S)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-2-methylhexanoic acid;MFCD32263502;PB48168;CS-0312269;F81076;
Fmoc-2-Me-Nle-OH, also known as Fmoc-2-methyl-norleucine, is a synthetic amino acid derivative widely utilized in peptide chemistry and biochemical research. Structurally, it features an Fmoc (9-fluorenylmethyloxycarbonyl) protective group at the N-terminus and a methylated norleucine backbone, offering unique steric and hydrophobic properties compared to standard amino acids. As a non-natural building block, it provides researchers with expanded options for designing peptides with enhanced stability, altered conformational preferences, and tailored physicochemical characteristics, making it a valuable tool in the development of novel biomolecules and functional studies.
Peptide Synthesis: In solid-phase peptide synthesis (SPPS), Fmoc-2-Me-Nle-OH serves as a versatile building block for the incorporation of 2-methyl-norleucine residues into custom peptide sequences. Its Fmoc-protected structure is compatible with standard Fmoc-based SPPS protocols, enabling efficient stepwise elongation and deprotection cycles. The methyl substitution at the alpha carbon introduces steric bulk, which can influence peptide backbone conformation and enhance resistance to enzymatic degradation. Researchers leverage these properties to design peptides with improved metabolic stability or to probe structure-activity relationships in sequence-variant libraries.
Conformational Analysis: The introduction of 2-methyl-norleucine into peptides using this derivative allows for systematic exploration of backbone flexibility and secondary structure formation. By substituting canonical amino acids with this methylated analog, scientists can investigate the effects of side-chain bulk and hydrophobicity on helix propensity, beta-sheet stability, or turn formation. These studies are instrumental in understanding the determinants of peptide folding and in engineering sequences with desired conformational features for applications in molecular recognition, catalysis, or material science.
Protease Resistance Studies: Incorporating Fmoc-2-Me-Nle-OH into peptide chains is a common strategy to enhance proteolytic stability. The presence of the 2-methyl group can hinder access by proteases, thereby prolonging peptide half-life in biological assays or in vitro systems. This approach is particularly valuable in the development of peptide-based probes, substrates, or modulators that require sustained activity in protease-rich environments. Such modifications enable more reliable experimental outcomes by minimizing degradation-related variability.
Peptidomimetic Design: The non-natural nature of 2-methyl-norleucine makes it a useful component in the synthesis of peptidomimetics—molecules that mimic the structure and function of natural peptides but exhibit improved stability or altered biological properties. By introducing this residue via Fmoc-2-Me-Nle-OH, researchers can modulate hydrophobicity, steric profile, and side-chain interactions within designed scaffolds. These modifications support the development of novel ligands, inhibitors, or molecular tools for probing protein-protein interactions, signaling pathways, or receptor binding events.
Analytical Method Development: The distinct physicochemical characteristics of peptides containing 2-methyl-norleucine make them suitable as reference standards or model compounds in analytical method development. Their unique retention behavior and mass spectral signatures aid in optimizing chromatographic separation conditions, validating mass spectrometry protocols, or calibrating peptide quantification assays. Utilizing such modified peptides enhances the robustness and specificity of analytical workflows in peptide research and quality control environments.
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