L-Lactolactoyl-Lys-Octreotide introduces a lactoyl modification onto a lysine side chain within octreotide, enhancing polarity and hydrogen-bond capacity. The additional moiety can modulate receptor binding and surface recognition. Researchers examine its effects on peptide conformation and transport properties. Applications include pro-moiety design, peptide-matrix interaction studies, and modified-analogue characterization.
CAT No: Z10-101-213
CAS No:2821715-05-1
Synonyms/Alias:D-Phenylalanyl - L-hemicystyl - L-phenylalanyl - D-tryptophyl -(N-L-Lactolactoyl) - L-lysyl -L-threonyl - L-hemicystyl - L-Threoninol cyclic (2-7) - disulfide; (R)-1-((4-((4R,7S,10S,13R,16S,19R)-13-((1H-indol-3-yl)methyl)-19-((R)-2-amino-3-phenylpropanamido)-16-benzyl-4-(((2R,3R)-1,3-dihydroxybutan-2-yl)carbamoyl)-7-((R)-1-hydroxyethyl)-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentaazacycloicosan-10-yl)butyl)amino)-1-oxopropan-2-yl(S)-2-hydroxypropanoate
L-Lactolactoyl-Lys-Octreotide is a synthetic peptide derivative that combines the structural features of octreotide, a somatostatin analog, with an N-terminal modification involving lactolactoyl-lysine. This compound is characterized by its tailored peptide backbone, which imparts unique physicochemical properties and potential for specialized biochemical applications. Its design enables researchers to explore peptide-ligand interactions, investigate structure-activity relationships, and develop new functional analogs for advanced studies in peptide chemistry and molecular pharmacology. The presence of both the modified lysine residue and the octreotide core provides a versatile platform for probing diverse biological and analytical contexts, making it a valuable tool in peptide-based research.
Peptide Structure-Activity Relationship Studies: The incorporation of a lactolactoyl-lysine moiety into the octreotide framework allows for detailed investigation of how N-terminal modifications impact peptide conformation, receptor affinity, and biological stability. Researchers utilize this compound to systematically assess the effects of structural alterations on peptide-receptor interactions, enabling the rational design of analogs with tailored properties. Such studies are critical for elucidating the determinants of peptide function and for optimizing bioactive peptides for research use.
Peptide Synthesis and Method Development: L-Lactolactoyl-Lys-Octreotide serves as a model substrate for evaluating synthetic strategies involving the introduction of non-standard amino acid modifications. Its complex structure provides a challenging yet informative template for testing coupling reagents, protecting group strategies, and purification techniques within solid-phase peptide synthesis workflows. This application is particularly relevant for peptide chemists aiming to expand the chemical diversity of synthetic peptides and improve the efficiency of incorporating modified residues.
Analytical Characterization and Method Validation: The unique physicochemical profile of this peptide derivative makes it an excellent standard for developing and validating analytical methods such as high-performance liquid chromatography (HPLC), mass spectrometry, and peptide mapping protocols. Laboratories employ it to calibrate instrumentation, assess method sensitivity and specificity, and establish reference parameters for detecting structurally similar analogs. Its defined structure and stability facilitate robust analytical performance in peptide quantification and identification assays.
Peptide-Protein Interaction Studies: L-Lactolactoyl-Lys-Octreotide is utilized as a probe in binding assays and biophysical studies aimed at understanding the molecular basis of peptide-protein interactions. The presence of both the octreotide core and the modified lysine residue enables researchers to explore how specific chemical modifications influence binding kinetics, thermodynamics, and selectivity. Such investigations contribute to a deeper understanding of ligand recognition and inform the design of novel peptide ligands for research applications.
Conjugation and Bioconjugate Research: The functional groups present in this synthetic peptide facilitate its use as a scaffold for bioconjugation experiments. Scientists leverage its chemical versatility to attach fluorophores, affinity tags, or other biomolecules, generating conjugates for imaging, affinity purification, or molecular tracking studies. These applications are essential for advancing peptide-based labeling techniques and for developing multifunctional research tools in molecular biology and analytical biochemistry.
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