If you are looking to purchase high quality KPV peptide for your research or therapeutic purposes, you have come to the right place. Our selection of KPV peptides is designed to meet stringent standards for purity and potency, ensuring reliable results in every experiment. By choosing our product, you can be confident that each batch has undergone rigorous testing, including mass spectrometry confirmation and HPLC purification, to verify its identity and integrity.
Shop our Full Range of KPV Peptides
We offer a comprehensive catalog of KPV peptides tailored to different needs. Whether you require the standard KPV sequence for basic studies or a modified version with enhanced stability, we have options available. Our full range includes:
Standard KPV (Lys-Pro-Val) peptide in lyophilized form
Modified KPV variants with D-amino acid substitutions for increased resistance to proteases
C-terminal amidated versions that mimic physiological conditions more closely
Peptide conjugates designed for targeted delivery or imaging
Each product is packaged with detailed documentation, including recommended storage conditions and usage guidelines. Our inventory is regularly updated to reflect the latest research developments and customer demand.
Structure of KPV Peptide
KPV peptide is a tripeptide composed of lysine (Lys), proline (Pro), and valine (Val). The amino acid sequence follows a linear arrangement: Lysine at the N-terminus, followed by Proline, and ending with Valine. The side chain of lysine carries a positively charged ε-amino group that can interact electrostatically with negatively charged biological membranes or receptors. Proline introduces a rigid cyclic structure that often imposes conformational constraints, potentially influencing binding affinity or proteolytic resistance. Valine provides hydrophobic character, aiding in membrane interactions and contributing to the overall amphipathic nature of the peptide.
In solution, KPV typically adopts an extended conformation, though its short length allows for rapid folding into a compact structure under certain conditions. The presence of proline disrupts typical α-helical or β-sheet formations, making KPV unique among small peptides in its ability to engage specific receptors without forming extensive secondary structures. This property is central to its reported anti-inflammatory and immunomodulatory activities.
By understanding the detailed composition and structural nuances of KPV peptide, researchers can better design experiments that leverage its unique properties for therapeutic exploration or basic science investigations.
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