VPM Peptide contains a defined protease-sensitive sequence often used as a cleavable linker in biomaterial and drug-delivery studies. Residue arrangement provides control over susceptibility to matrix metalloproteinases. Researchers investigate cleavage kinetics and structural stability within crosslinked networks. Applications include responsive hydrogel design, targeted-release systems, and enzyme-degradable scaffolds.
CAT No: R2394
CAS No:1428885-83-9
Synonyms/Alias:VPM peptide;1428885-83-9;AKOS040756792;DA-78918;
VPM peptide is a synthetic tripeptide composed of valine, proline, and methionine, recognized for its utility in peptide research and biochemical studies. As a short-chain peptide, it serves as a model system for investigating peptide bond formation, stability, and structure-activity relationships. Its defined sequence and physicochemical properties make it valuable for probing enzymatic specificity, substrate recognition, and the fundamental principles governing peptide behavior in biological and chemical systems. Researchers utilize VPM peptide in diverse experimental frameworks to elucidate mechanisms of proteolysis, peptide transport, and the interplay between amino acid sequence and molecular function.
Peptide substrate studies: In enzymology, VPM peptide functions as a substrate for protease activity assays, particularly those involving enzymes with specificity for short, hydrophobic, or sulfur-containing sequences. Its defined tripeptide structure enables precise assessment of proteolytic cleavage patterns, providing insight into enzyme kinetics, substrate preference, and active site selectivity. This information is critical for characterizing novel proteases, optimizing assay conditions, and advancing understanding of protein turnover and degradation pathways.
Peptide synthesis optimization: The tripeptide is routinely employed as a benchmark in solid-phase peptide synthesis (SPPS) and solution-phase peptide assembly protocols. Its sequence allows researchers to evaluate coupling efficiency, resin compatibility, and the impact of sequence composition on synthetic yield and purity. By serving as a representative model, it aids in troubleshooting synthetic challenges, refining deprotection strategies, and validating new chemistries or reagents used in peptide manufacturing.
Analytical method development: VPM peptide is frequently utilized as a calibration or reference standard in chromatographic and mass spectrometric analyses. Its well-characterized mass and retention properties facilitate the development, validation, and quality control of analytical methods for peptide quantification and identification. Analytical laboratories employ it to assess instrument response, optimize separation parameters, and ensure reproducibility in peptide profiling workflows.
Structural and conformational studies: The tripeptide serves as a model compound for investigating peptide secondary structure, folding, and conformational dynamics using spectroscopic techniques such as NMR, circular dichroism, and infrared spectroscopy. Its simple yet representative sequence enables fundamental research into the effects of side-chain composition and peptide length on molecular flexibility, hydrogen bonding, and intramolecular interactions. These studies contribute to broader understanding of peptide structure-function relationships and inform the design of bioactive peptides.
Peptide transport and uptake research: In cellular and biochemical experiments, VPM peptide is used to probe mechanisms of peptide uptake, transport, and intracellular processing. Its manageable size and defined sequence allow for controlled studies on peptide permeation across biological membranes, transporter specificity, and cellular uptake kinetics. Such investigations are essential for elucidating the principles governing peptide delivery, stability, and bioavailability in research models, supporting the development of peptide-based probes and delivery systems.
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
4. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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