Ac-Met-Ala-Ser-OH is a tripeptide containing sulfur, aliphatic, and polar residues arranged to explore backbone flexibility and oxidative sensitivity. Researchers use it to study peptide-protein contacts, solvent interactions, and enzymatic processing. The acetylated N-terminus stabilizes the sequence during structural analysis. Its minimal structure supports precise mechanistic evaluation.
CAT No: R2307
CAS No:149151-19-9
Synonyms/Alias:Ac-Met-Ala-Ser-OH;149151-19-9;(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-4-methylsulfanylbutanoyl]amino]propanoyl]amino]-3-hydroxypropanoic acid;FA109730;
Ac-Met-Ala-Ser-OH, also known as N-acetyl-methionyl-alanyl-serine, is a synthetic tripeptide featuring an acetylated N-terminus and a free carboxyl group at the C-terminus. This peptide is designed to offer enhanced stability and bioavailability due to its acetyl modification, making it a valuable tool in various biochemical and life science research applications. Its unique sequence, comprising methionine, alanine, and serine, provides a versatile platform for studying peptide interactions, enzymatic processes, and signaling pathways. The presence of methionine introduces a sulfur-containing amino acid, which can be critical in redox reactions and protein function studies, while serine's hydroxyl group offers opportunities for phosphorylation and other post-translational modification research. The compact and well-defined structure of Ac-Met-Ala-Ser-OH allows for precise control in experimental design, facilitating its use in peptide mapping, structural biology, and functional assays.
Peptide Mapping and Proteomics: In proteomic research, Ac-Met-Ala-Ser-OH serves as a reference standard or model substrate for peptide mapping experiments aimed at elucidating protease specificity and cleavage patterns. Researchers utilize this tripeptide to calibrate analytical techniques such as mass spectrometry and HPLC, enabling accurate identification and quantification of peptide fragments derived from complex biological mixtures. By incorporating this synthetic sequence into mapping protocols, scientists can validate enzymatic digestion efficiency and optimize conditions for protein characterization studies.
Enzyme Substrate Studies: As a defined tripeptide, N-acetyl-methionyl-alanyl-serine is widely used as a substrate for investigating the activity of exopeptidases, amidases, and other proteolytic enzymes. Its acetylated N-terminus prevents non-specific degradation, ensuring that enzymatic reactions can be monitored with high specificity. By analyzing the cleavage products generated from this peptide, researchers gain insights into enzyme kinetics, substrate preferences, and the mechanisms underlying peptide bond hydrolysis, supporting the development of novel enzyme inhibitors or activators.
Signal Transduction Research: The sequence Met-Ala-Ser is relevant in the context of cellular signaling pathways, particularly those involving serine phosphorylation and methionine oxidation. Scientists employ Ac-Met-Ala-Ser-OH to mimic motifs found in endogenous proteins, enabling studies of kinase and phosphatase activity, post-translational modifications, and protein-protein interactions. Through these investigations, the peptide aids in unraveling the molecular basis of signal transduction events and the regulatory roles of specific amino acid residues within signaling cascades.
Structural Biology and Conformational Analysis: The well-defined structure of Ac-Met-Ala-Ser-OH makes it a valuable model for conformational studies using NMR spectroscopy, circular dichroism, and computational modeling. By examining its three-dimensional folding and dynamics, researchers can explore the factors influencing peptide stability, secondary structure formation, and intramolecular interactions. This knowledge contributes to the rational design of bioactive peptides, peptidomimetics, and small-molecule modulators targeting protein interfaces.
Peptide Modification and Synthesis Research: The utility of N-acetyl-methionyl-alanyl-serine extends to peptide chemistry, where it serves as a template for studying chemical modifications such as acetylation, methylation, and phosphorylation. Synthetic chemists use this tripeptide to optimize coupling reactions, protecting group strategies, and purification techniques. Its modular structure allows for the introduction of labels, tags, or other functional groups, facilitating the creation of customized peptide probes and analytical standards for downstream applications.
Biomaterials and Surface Functionalization: In materials science, Ac-Met-Ala-Ser-OH is explored as a building block for functionalizing biomaterial surfaces and developing peptide-based coatings. Its sequence can be grafted onto polymers, nanoparticles, or sensor platforms to impart bioactivity, enhance biocompatibility, or promote specific molecular recognition events. These applications are particularly relevant in the design of biosensors, tissue engineering scaffolds, and drug delivery systems, where tailored peptide surfaces improve performance and enable targeted interactions with biological systems. Through these diverse application directions, Ac-Met-Ala-Ser-OH demonstrates its versatility and scientific value across multiple research disciplines.
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