Ac-Leu-NH2 contains the leucine side chain (isobutyl) attached to an N-acetylated amino acid framework, forming an amino acid amide rather than a free amino acid. The molecule bears an N-acetyl protecting group on the α-amino functionality and an amide at the α-carboxyl position (-C(=O)NH2), which reduces carboxyl reactivity and maintains a defined terminal amide for controlled coupling behavior. Ac-Leu-NH2 is used as a peptide-related intermediate or building block in peptide chemistry and analytical method development where a leucine residue with a terminal primary amide is required for further derivatization or fragment assembly.
CAT No: CP26955
CAS No:28529-34-2
Synonyms/Alias:AC-LEU-NH2;28529-34-2;(2S)-2-acetamido-4-methylpentanamide;30130-37-1;Acetyl-L-leucineamide;N-Acetyl-D-leucineamide;AC1Q1OAI;N-acetyl-L-leucineamide;N-Acetyl-D-leucineamide;AC1L3G9A;Nalpha-Acetyl-L-leucinamide;SCHEMBL7669779;MolPort-001-833-353;ZINC399348;16624-68-3;6095AH;AKOS024337851;AK187104;OR228954;K-7255;PENTANAMIDE,2-(ACETYLAMINO)-4-METHYL-,(2R)-
Ac-Leu-NH2 is an N-acetylated leucine amide that provides a protected, peptide-like C-terminal amide functionality while retaining the leucine side chain for hydrophobic interaction studies. As a small, well-defined amino acid derivative, it is frequently used as a model substrate and reference compound in peptide chemistry, chemical biology, and analytical method development where a leucine-containing motif is required without introducing additional reactive termini. Its amide end-group and N-acetyl cap make it particularly useful for probing recognition and processing events that depend on backbone and terminal chemistry rather than free amino and carboxyl groups.
1. Peptide Substrate Modeling
Ac-Leu-NH2 is used as a compact leucine-containing substrate or mimic in enzymology and peptide chemistry workflows that evaluate how terminal capping and C-terminal amide features influence processing. Researchers commonly employ this type of acylated amino acid amide to benchmark cleavage or binding behavior in assays where free amino and carboxyl groups would otherwise introduce non-specific interactions or complicate interpretation. In peptide-based chemical biology, it also serves as a convenient standard for comparing responses across related N-acylated or C-terminally amidated structures.
2. Protease Activity Reference
Ac-Leu-NH2 supports protease and peptidase activity studies by providing a defined backbone context with a leucine side chain and a non-ionizable terminal amide. In practice, it is used by assay developers and analytical chemists to establish baseline reactivity, calibrate readouts, or validate assay selectivity when screening substrate libraries that include leucine motifs. Because the N-acetyl group suppresses the reactivity of the amino terminus, it helps isolate the contribution of the peptide bond environment and the C-terminal amide in mechanistic or comparative studies.
3. LC-MS and Chromatography Standards
Ac-Leu-NH2 is a practical reference material for LC-MS and chromatographic method development targeting peptide-like small molecules and amino acid amide species. Analytical teams use it to tune retention behavior, confirm identity via mass spectral features, and support quantitation workflows that require stable, well-characterized standards. Its defined acetylated N-terminus and C-terminal amide make it a useful calibration compound when monitoring enzymatic reactions, degradation products, or synthetic intermediates that produce leucine-containing acylated amides.
4. Building Block for Peptidomimetics
Ac-Leu-NH2 is also used as a starting building block in peptidomimetic and small-molecule design efforts where a leucine-derived hydrophobic element and an amide-capable backbone are required. Medicinal chemistry and chemical biology groups incorporate this motif into larger synthetic sequences to generate defined peptide-like fragments for structure-activity relationship studies or binding assays. The capped, non-zwitterionic character of the amide derivative helps maintain consistent handling in synthesis and downstream analytical characterization compared with free amino acid forms.
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