Fmoc-Ala-Glu-Asn-Lys-NH2 combines a protecting group with a functional tetrapeptide used in synthetic route optimization. Acidic, neutral, and basic residues create a well-balanced system for conformational assessment. The C-terminal amide supports stability during coupling and deprotection steps. Researchers apply it to resin-bound synthesis testing, sequence expansion, and bioconjugation strategy evaluation.
CAT No: R2327
CAS No:220701-06-4
Synonyms/Alias:Fmoc-Ala-Glu-Asn-Lys-NH2;220701-06-4;AKOS040756234;MS-31095;HY-114174;CS-0078435;G17225;(4S)-5-[[(2S)-4-amino-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-4-[[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoyl]amino]-5-oxopentanoic acid;
Fmoc-Ala-Glu-Asn-Lys-NH2 is a synthetic tetrapeptide protected at the N-terminus with a fluorenylmethyloxycarbonyl (Fmoc) group and capped at the C-terminus with an amide. As a custom-sequence peptide, it features a specific arrangement of alanine, glutamic acid, asparagine, and lysine residues, making it a valuable building block for advanced peptide synthesis and structure-function studies. The Fmoc protection facilitates solid-phase peptide synthesis (SPPS), while the C-terminal amidation enhances the mimicry of native protein fragments and improves stability against enzymatic degradation. Its defined sequence and terminal modifications allow researchers to explore diverse biochemical and biophysical properties, supporting a range of applications in molecular biology, medicinal chemistry, and protein engineering research.
Peptide Synthesis: Fmoc-Ala-Glu-Asn-Lys-NH2 serves as a key intermediate for the stepwise assembly of longer peptide chains using Fmoc-based SPPS protocols. The Fmoc group provides orthogonal protection, enabling precise deprotection and coupling cycles without interfering with side-chain functionalities. This tetrapeptide is particularly useful for synthesizing custom peptides with specific sequence motifs, facilitating the generation of libraries or the incorporation of functional domains into larger biomolecules for downstream applications.
Protein-Protein Interaction Studies: The defined sequence and terminal modifications of this tetrapeptide make it suitable for probing protein-protein interactions, especially in studies aimed at mapping binding sites or elucidating recognition motifs. By incorporating it into binding assays or surface plasmon resonance experiments, researchers can investigate the specificity and affinity of interactions with target proteins, contributing to a deeper understanding of molecular recognition events in cellular pathways.
Structure-Activity Relationship (SAR) Analysis: The peptide's sequence, featuring both polar and charged residues, is ideal for SAR studies designed to dissect the role of individual amino acids in biological activity. By systematically modifying or substituting residues within the sequence, scientists can assess the impact on function, stability, or binding, thereby informing the rational design of more potent or selective peptide analogs for research and development purposes.
Biophysical Characterization: The amide-capped tetrapeptide is well-suited for biophysical analyses, such as circular dichroism (CD) spectroscopy or nuclear magnetic resonance (NMR) studies, to investigate secondary structure propensity and conformational dynamics. Its defined length and composition enable the exploration of sequence-dependent folding behavior, aggregation tendencies, or interaction with lipid membranes, providing insights into the fundamental properties of short peptide segments.
Peptide Functionalization and Conjugation: The free side chains and terminal modifications of Fmoc-Ala-Glu-Asn-Lys-NH2 offer versatile handles for further chemical derivatization or conjugation to other biomolecules, fluorophores, or solid supports. This capability is valuable in the development of peptide-based probes, affinity tags, or immobilized ligands for affinity purification, biosensor construction, or targeted delivery systems in analytical and preparative research workflows.
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