pep2-AVKI

Selective peptide inhibitor of GluR2 subunit (at the C-terminal PDZ site) binding to PICK1, which does not have an effect on binding of GluA2 to GRIP or ABP, and does not increase AMPA current amplitude or affect long term depression (LTD).

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R0919

CAS No:1315378-69-8

Custom Peptide Synthesis
cGMP Peptide
  • Registration of APIs
  • CMC information required for an IND
  • IND and NDA support
  • Drug master files (DMF) filing
M.F/Formula
C60H93N13O17
M.W/Mr.
1268.47
Sequence
YNVYGIEAVKI
Labeling Target
AMPA receptor (GluR2)
Appearance
White lyophilised solid
Purity
>98%
Activity
Inhibitor

pep2-AVKI is a synthetic peptide compound designed for advanced research applications in the fields of molecular biology, cellular signaling, and biochemical pathway analysis. As a custom-engineered peptide sequence, it serves as a valuable tool for probing protein-protein interactions, modulating signaling cascades, and elucidating the functional roles of specific peptide motifs in diverse biological systems. Its defined sequence and high degree of specificity make it particularly useful for mechanistic studies where precise molecular targeting is essential. Researchers leverage such peptides to dissect complex biological phenomena, enabling new insights into cellular processes and molecular mechanisms.

Protein-protein interaction studies: Synthetic peptides like pep2-AVKI are widely employed as molecular probes to investigate and characterize protein-protein interactions. By mimicking or disrupting native binding motifs, this peptide can be used to map interaction domains, identify critical residues involved in binding, and assess the selectivity of protein complexes. Such studies are fundamental for understanding cellular signaling networks and for developing targeted strategies to modulate these interactions in vitro.

Signal transduction research: In the context of cell signaling, peptides with defined sequences provide a controlled means to modulate or inhibit specific pathways. pep2-AVKI can be introduced into cell lysates or model systems to interfere with or mimic endogenous peptide sequences, thereby helping to delineate the contribution of particular motifs to signal propagation. This approach is instrumental in identifying key nodes within signaling cascades and in validating potential drug targets at the molecular level.

Enzyme substrate analysis: Custom peptides serve as substrates in enzymatic assays to evaluate the specificity and activity of proteases, kinases, or other modifying enzymes. The sequence of pep2-AVKI can be tailored to match consensus motifs recognized by target enzymes, allowing researchers to monitor catalytic activity, substrate preference, and kinetic parameters under controlled experimental conditions. Such analyses are essential for enzyme characterization and for screening potential inhibitors in drug discovery research.

Peptide-functional studies: The unique sequence of pep2-AVKI enables its use in functional assays designed to probe the biological activity of peptide motifs. Researchers may employ this peptide to assess effects on cellular processes such as migration, adhesion, or differentiation, depending on the biological context. By systematically varying the concentration or sequence, it is possible to uncover structure-activity relationships and to identify minimal motifs required for activity, supporting rational design of bioactive peptides.

Analytical method development: Synthetic peptides like pep2-AVKI are frequently utilized as standards or calibration references in mass spectrometry, HPLC, and other analytical platforms. Their defined composition and stability make them ideal for method validation, quantification of peptide analytes, or optimization of detection parameters. This application is critical for ensuring accuracy and reproducibility in proteomic workflows and for supporting quality control in peptide-based research and manufacturing environments.

Solubility
-20 °C
InChI
InChI=1S/C60H93N13O17/c1-10-32(7)49(59(88)67-41(23-24-46(78)79)54(83)65-34(9)51(80)71-47(30(3)4)57(86)66-40(14-12-13-25-61)55(84)73-50(60(89)90)33(8)11-2)70-45(77)29-64-53(82)42(27-36-17-21-38(75)22-18-36)69-58(87)48(31(5)6)72-56(85)43(28-44(63)76)68-52(81)39(62)26-35-15-19-37(74)20-16-35/h15-22,30-34,39-43,47-50,74-75H,10-14,23-29,61-62H2,1-9H3,(H2,63,76)(H,64,82)(H,65,83)(H,66,86)(H,67,88)(H,68,81)(H,69,87)(H,70,77)(H,71,80)(H,72,85)(H,73,84)(H,78,79)(H,89,90)/t32-,33-,34-,39-,40-,41-,42-,43-,47-,48-,49-,50-/m0/s1
InChI Key
SODUKHPKIVEQLX-OCXIBOJYSA-N
Isomeric SMILES
CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)O)NC(=O)CNC(=O)[C@H](CC1=CC=C(C=C1)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC2=CC=C(C=C2)O)N

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