H-Lys-Gly-OH.HCl

H-Lys-Gly-OH.HCl, also known as Lysylglycine hydrochloride, is a dipeptide consisting of L-lysine and glycine linked via a peptide bond and presented as its hydrochloride salt. As a synthetic peptide fragment, it serves as a fundamental building block in peptide chemistry and biochemical research, offering unique properties derived from the side-chain reactivity of lysine and the structural flexibility of glycine. Its modular structure makes it a valuable tool for probing peptide function, facilitating structure-activity relationship studies, and supporting the development of peptide-based technologies. Researchers leverage its defined sequence and physicochemical characteristics to advance investigations in protein engineering, enzymology, and analytical biochemistry.

Peptide synthesis: Lysylglycine hydrochloride is frequently employed as a protected or activated intermediate in solid-phase and solution-phase peptide synthesis. Its incorporation into growing peptide chains allows for precise control over sequence assembly, enabling the generation of custom peptides for research and development purposes. The presence of lysine introduces a reactive side chain that can be further modified or conjugated, while glycine imparts conformational flexibility, making the dipeptide particularly useful for synthesizing peptides with tailored biochemical properties.

Enzyme substrate studies: The dipeptide serves as a model substrate for peptidase and protease assays, aiding in the characterization of enzyme specificity, kinetics, and mechanism. By utilizing this compound in controlled enzymatic reactions, researchers can investigate substrate recognition motifs and catalytic preferences, which are critical for understanding proteolytic processes in biological systems. The defined sequence of lysylglycine facilitates the interpretation of enzymatic cleavage patterns and supports the development of selective inhibitors or activity probes.

Peptide transport and uptake research: Due to its simple structure, lysylglycine hydrochloride is utilized in studies of peptide transporters and membrane permeability. Investigations into the uptake and translocation of small peptides across cellular membranes rely on model compounds like this dipeptide to elucidate the molecular determinants of transporter specificity and function. Such studies are essential for advancing knowledge in nutrient absorption, drug delivery, and cellular signaling pathways involving oligopeptide transport.

Analytical method development: The compound is often used as a reference standard or calibration material in chromatographic and mass spectrometric analyses of peptides. Its well-defined mass and chemical characteristics facilitate the validation and optimization of analytical workflows, including peptide mapping, purity assessment, and quantification. Employing lysylglycine hydrochloride as a benchmark supports the reliability and reproducibility of peptide analysis in research and industrial laboratories.

Structure-activity relationship (SAR) investigations: Incorporation of this dipeptide into peptide libraries or as a motif in larger biomolecules enables systematic SAR studies. Researchers can probe the influence of lysine's basic side chain and glycine's minimal steric hindrance on biological activity, binding affinity, or conformational stability. These insights are instrumental in guiding the rational design of peptide-based ligands, inhibitors, or scaffolds for applications in biochemistry, molecular biology, and chemical biology.

1. Immune responses to peptides containing homocitrulline or citrulline in the DR4-transgenic mouse model of rheumatoid arthritis

2. Uncarboxylated osteocalcin decreases insulin-stimulated glucose uptake without affecting insulin signaling and regulators of mitochondrial biogenesis in myotubes

3. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

4. Effect of Short-Term Desiccation, Recovery Time, and CAPA-PVK Neuropeptide on the Immune System of the Burying Beetle Nicrophorus vespilloides

5. TMEM16F and dynamins control expansive plasma membrane reservoirs