H-Met-Ala-Ser-Met-Thr-Gly-Gly-Gln-Gln-Met-Gly-OH contains three methionine residues that introduce multiple thioether sites for oxidation and metal coordination studies. Polar serine, threonine, and glutamine residues modulate solubility and hydrogen bonding. Researchers use the peptide to probe oxidative stress, sulfoxide formation, and conformational shifts. Applications include redox biochemistry, peptide-stability analysis, and sulfur-containing motif design.
CAT No: PI-018
CAS No:245445-88-9
Synonyms/Alias:T7 Tag Peptide;245445-88-9;G13552;
H-Met-Ala-Ser-Met-Thr-Gly-Gly-Gln-Gln-Met-Gly-OH is a synthetic peptide composed of eleven amino acid residues arranged in a specific sequence. As a linear oligopeptide, it serves as a valuable tool in biochemical research for investigating peptide structure-function relationships, protein-protein interactions, and post-translational modification pathways. Its defined sequence allows for precise experimental control, making it suitable for a variety of applications where sequence specificity and peptide stability are critical. The presence of multiple methionine, glycine, and glutamine residues imparts unique physicochemical properties, offering opportunities to study redox sensitivity, aggregation behavior, and enzymatic processing relevant to both fundamental and applied peptide science.
Peptide structure-activity relationship studies: Researchers frequently employ this peptide in systematic investigations to delineate the correlation between primary sequence and biological activity. By substituting or modifying specific residues within the sequence, scientists can assess the impact on conformation, receptor binding, or enzymatic susceptibility. Such studies contribute to the rational design of bioactive peptides and the identification of critical motifs responsible for functional outcomes in cellular or biochemical assays.
Enzymatic substrate evaluation: The defined sequence of this oligopeptide makes it an ideal substrate for exploring the specificity and kinetics of various proteolytic enzymes, including endopeptidases and exopeptidases. By monitoring cleavage patterns and rates, investigators can characterize enzyme selectivity, map cleavage sites, and develop assays for high-throughput screening of protease inhibitors or activators. The inclusion of methionine residues also allows for targeted studies involving methionine oxidation or S-adenosylmethionine-dependent modifications.
Peptide-based assay development: Synthetic peptides such as this one are widely used as standards or calibrators in quantitative biochemical assays, including enzyme-linked immunosorbent assays (ELISA), mass spectrometry-based quantification, and biosensor platforms. The reproducibility and purity of the sequence support reliable assay performance, enabling accurate detection, quantification, or monitoring of specific analytes in complex biological samples.
Protein-peptide interaction analysis: The sequence provides a platform for studying non-covalent interactions between peptides and target proteins, which are central to many cellular processes. Surface plasmon resonance, isothermal titration calorimetry, and co-immunoprecipitation techniques can utilize this peptide to probe binding affinities, map interaction domains, or identify novel protein partners. Insights gained from such experiments inform the development of peptide-based modulators or inhibitors with potential research utility.
Peptide aggregation and stability research: The presence of glycine and glutamine-rich motifs within the sequence makes it a suitable model for investigating peptide aggregation, fibril formation, and solubility under various physiological or stress conditions. These studies are relevant for understanding mechanisms underlying protein misfolding, amyloidogenesis, and the design of aggregation-resistant peptide therapeutics. Experimental manipulation of environmental factors such as pH, ionic strength, or oxidative stress can reveal critical determinants of peptide stability and inform formulation strategies for peptide-based reagents.
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