Isoleucyl-lysyl-valyl-alanyl-valine blends hydrophobic residues with a basic lysine, forming a sequence that highlights charge-hydrophobic balance. The peptide supports exploration of secondary-structure initiation and intermolecular association. Researchers assess its hydrogen-bond patterns in varied environments. Applications include motif analysis, peptide assembly research, and folding studies.
CAT No: R2471
CAS No:131167-89-0
Synonyms/Alias:131167-89-0;IKVAV;Ile-lys-val-ala-val;H-Ile-Lys-Val-Ala-Val-OH;Isoleucyl-lysyl-valyl-alanyl-valine;L-Valine,L-isoleucyl-L-lysyl-L-valyl-L-alanyl-;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]propanoyl]amino]-3-methylbutanoic acid;SCHEMBL180642;CHEMBL1904201;DTXSID40927101;HY-P4322;N-(N-(N-(N(2)-L-Isoleucyl-L-lysyl)-L-valyl)-L-alanyl)-L-valine;NCGC00167208-01;DA-74166;CS-0653507;H-Ile-Lys-Val-Ala-Val-OH trifluoroacetate salt;L-Valine, N-(N-(N-(N(2)-L-isoleucyl-L-lysyl)-L-valyl)-L-alanyl)-;N-(2-{[2-({6-Amino-2-[(2-amino-1-hydroxy-3-methylpentylidene)amino]-1-hydroxyhexylidene}amino)-1-hydroxy-3-methylbutylidene]amino}-1-hydroxypropylidene)valine;
Isoleucyl-lysyl-valyl-alanyl-valine is a synthetic pentapeptide composed of the amino acids isoleucine, lysine, valine, alanine, and valine arranged in a specific sequence. As a structurally defined oligopeptide, it serves as a valuable tool for investigating peptide-related biochemical processes, including protein-protein interactions, enzymatic specificity, and structural biology. Its design enables researchers to explore the functional consequences of sequence variation, side-chain diversity, and backbone conformation on peptide behavior in a variety of experimental contexts. The presence of both hydrophobic and basic residues within this sequence makes it particularly relevant for model studies of peptide folding, substrate recognition, and intermolecular binding events.
Peptide substrate studies: In enzymology research, this pentapeptide is frequently utilized as a model substrate to assess the activity and specificity of proteolytic enzymes such as endopeptidases and exopeptidases. By monitoring the cleavage patterns and reaction kinetics, scientists can elucidate enzyme selectivity, catalytic mechanisms, and substrate preferences. The defined sequence of isoleucyl-lysyl-valyl-alanyl-valine allows for precise mapping of cleavage sites and supports the development of quantitative assays for enzyme characterization.
Peptide structure-function analysis: The sequence diversity within this pentapeptide supports investigations into the relationship between primary structure and biological function. Researchers employ it in conformational studies using techniques such as circular dichroism, NMR spectroscopy, or X-ray crystallography to examine secondary structure formation, backbone flexibility, and the influence of side-chain composition. Such studies are critical for understanding the determinants of peptide stability, folding pathways, and the impact of sequence motifs on molecular recognition.
Synthetic peptide chemistry: Isoleucyl-lysyl-valyl-alanyl-valine is widely used as a reference or test sequence in the optimization of solid-phase peptide synthesis protocols. Its moderate length and varied side-chain functionalities provide a practical model for evaluating coupling efficiency, protecting group strategies, and purification workflows. Peptide chemists leverage it to validate new synthetic methodologies, troubleshoot reaction conditions, and benchmark the performance of resins and reagents in laboratory-scale or automated synthesis platforms.
Peptide-membrane interaction studies: The amphipathic nature of this pentapeptide, featuring both hydrophobic and basic residues, makes it suitable for probing peptide-membrane interactions. In biophysical and cell-free systems, it is employed to assess membrane binding affinity, insertion depth, and the role of sequence composition in modulating membrane perturbation. Such experiments yield insights into the principles governing peptide association with lipid bilayers, which is relevant for understanding antimicrobial peptide mechanisms, signal transduction, and membrane protein targeting.
Analytical method development: As a well-characterized synthetic peptide, isoleucyl-lysyl-valyl-alanyl-valine serves as a calibration standard or quality control reference in analytical workflows such as high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Its defined mass, sequence, and physicochemical properties allow for the validation of chromatographic separation, detection sensitivity, and instrument performance. Analytical laboratories rely on such model peptides to ensure reproducibility, accuracy, and robustness in peptide quantification and identification protocols.
2. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
5. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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