Lys-Hyp-Gly-Glu-Pro-Gly-Pro-Lys-Gly mimics collagen-like motifs through hydroxyproline, glycine, and proline repeats. Terminal lysines introduce positive charge for matrix or receptor interactions. The sequence supports formation of ordered secondary structure under appropriate conditions. Researchers employ it to model extracellular-matrix segments, study cell-matrix adhesion, and evaluate protease sensitivity.
CAT No: R2601
CAS No:81100-00-7
Synonyms/Alias:EX-A9236;Lys-Hyp-Gly-Glu-Pro-Gly-Pro-Lys-Gly;81100-00-7;
Lys-Hyp-Gly-Glu-Pro-Gly-Pro-Lys-Gly is a synthetic peptide composed of nine amino acid residues, featuring a sequence that incorporates both basic and hydroxyproline-containing motifs. As a structurally defined oligopeptide, it serves as a valuable tool for researchers investigating peptide structure-function relationships, sequence-specific interactions, and the role of modified residues such as hydroxyproline in biochemical processes. The presence of both lysine and hydroxyproline within the sequence reflects motifs commonly found in extracellular matrix proteins, rendering this compound particularly relevant for studies related to protein engineering, biomolecular recognition, and peptide-based material science.
Peptide structure-function analysis: Researchers utilize this nonapeptide to dissect the contribution of individual amino acid residues—such as hydroxyproline and glutamic acid—to the overall conformation and bioactivity of short peptides. By systematically modifying or substituting positions within the sequence, scientists can elucidate how specific side chains influence secondary structure formation, stability, and molecular interactions, thereby advancing the fundamental understanding of peptide folding and function.
Protein-protein interaction modeling: The defined sequence of this peptide allows it to serve as a model system for probing sequence-dependent binding events and intermolecular recognition. It can be employed in assays aimed at characterizing the affinity and specificity of protein domains, antibodies, or enzymes that interact with lysine- or hydroxyproline-rich motifs. Such studies are critical for mapping interaction networks and for the rational design of peptide-based probes or inhibitors.
Biomaterials and scaffold development: Owing to its structural resemblance to motifs found in collagen and other extracellular matrix components, this oligopeptide is often incorporated into biomaterial research. It can be used to functionalize surfaces, hydrogels, or scaffolds, thereby imparting bioactive cues that promote cell adhesion, proliferation, or differentiation in tissue engineering and regenerative medicine research. The sequence's unique combination of charged and hydroxylated residues provides tunable properties for optimizing material-cell interactions.
Analytical method development: The well-defined nature and unique sequence of this peptide make it a useful standard or reference in analytical techniques such as mass spectrometry, high-performance liquid chromatography, and capillary electrophoresis. It aids in method calibration, validation, and optimization by providing a reproducible analyte for assessing peptide detection sensitivity, fragmentation patterns, and chromatographic behavior.
Peptide synthesis optimization: As a moderately complex sequence containing both standard and modified amino acids, this nonapeptide is frequently used as a test substrate in solid-phase peptide synthesis (SPPS) protocol development. Its incorporation of hydroxyproline and multiple glycine residues challenges synthesis conditions, allowing chemists to evaluate coupling efficiencies, resin compatibility, and deprotection strategies. Such applications are instrumental in refining methodologies for the efficient production of longer or more complex peptide targets.
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