SDGRG has been used as a control peptide which does not affect integrin function, in various studies
CAT No: 10-101-316
CAS No:108608-63-5
Synonyms/Alias:Ser-Asp-Gly-Arg-Gly;108608-63-5;DTXSID40405111;3-[(2-amino-3-hydroxypropanoyl)amino]-4-[[2-[[1-(carboxymethylamino)-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-4-oxobutanoic acid;DTXCID40355965;Ser-Asp-Gly-Arg-Gly, >=90% (HPLC);
Chemical Name:(3S)-3-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-4-[[2-[[(2S)-1-(carboxymethylamino)-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-4-oxobutanoic acid
SDGRG (Serine-Aspartic acid-Glycine-Arginine-Glycine) is a synthetic pentapeptide composed of a specific sequence of amino acids designed to mimic or modulate biological interactions in vitro. As a short peptide motif, SDGRG is of particular interest in biochemical research due to its potential to engage in protein-protein interactions, serve as a substrate or inhibitor in enzymatic assays, and act as a molecular probe in cellular signaling studies. The sequence itself is notable for incorporating both polar and basic residues, which can influence its binding properties and functional versatility in experimental systems. Researchers value such peptides for their utility in dissecting molecular pathways, validating target specificity, and expanding understanding of sequence-dependent biological effects.
Peptide interaction studies: SDGRG is frequently utilized in the investigation of peptide-protein and peptide-ligand interactions. Its defined sequence allows researchers to explore binding affinities and specific recognition patterns with various receptors, enzymes, or antibodies. By incorporating the pentapeptide into binding assays or surface plasmon resonance experiments, scientists can characterize the molecular determinants governing interaction specificity, which is fundamental for elucidating signaling pathways and molecular recognition events.
Enzyme substrate and inhibitor assays: The pentapeptide sequence serves as a valuable tool in enzymology, where it can be employed as a substrate or competitive inhibitor in protease activity assays. Its structural features, including the presence of arginine and aspartic acid residues, make it suitable for probing the substrate preferences of serine proteases, metalloproteases, or other peptide-cleaving enzymes. Through such applications, SDGRG enables precise quantification of enzyme kinetics, substrate specificity, and inhibitor efficacy.
Cell adhesion and migration research: Due to its amino acid composition, SDGRG is explored in cell adhesion and migration studies, particularly in the context of extracellular matrix (ECM) interactions. When immobilized on surfaces or incorporated into hydrogels, the peptide can influence cell attachment, spreading, and motility. This makes it a useful model for examining integrin-mediated signaling, cellular response to microenvironmental cues, and the development of biomimetic materials for tissue engineering research.
Peptide mapping and analytical method development: SDGRG is also employed as a standard or reference sequence in peptide mapping protocols and mass spectrometry-based analytical methods. Its well-defined structure and mass make it suitable for calibrating instrumentation, validating chromatographic separation techniques, and optimizing fragmentation parameters. Such applications are critical for ensuring the accuracy, reproducibility, and sensitivity of peptide-based analytical workflows in proteomics and quality control laboratories.
Peptide functionalization and conjugation studies: The unique sequence of SDGRG provides multiple functional groups amenable to chemical modification, making it an ideal candidate for conjugation experiments. Researchers can attach fluorescent probes, affinity tags, or bioactive moieties to specific residues, enabling the creation of multifunctional peptide constructs. These modified peptides are instrumental in the development of targeted delivery systems, biosensors, and molecular imaging tools, supporting innovation in both fundamental research and applied biotechnology.
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