Deamidated-Eptifibatide features a deamidated residue that alters charge distribution and hydrogen-bonding potential. Researchers examine its effects on conformational shifts and receptor-binding characteristics. Applications include impurity characterization, degradation mapping, and structural comparison.
CAT No: Z10-101-177
Synonyms/Alias:Deamidated Eptifibatide;618118-95-9;Deamidated Eptifibatide;L-Cysteine, N6-(aminoiminomethyl)-N2-(3-mercapto-1-oxopropyl)-L-lysylglycyl-L-a-aspartyl-L-tryptophyl-L-prolyl-, cyclic (1?6)-disulfide (9CI)
Deamidated-Eptifibatide is a synthetic peptide derivative structurally related to the well-characterized cyclic heptapeptide eptifibatide, which functions as a potent inhibitor of platelet aggregation. Featuring a deamidated residue modification, this compound offers researchers a valuable tool for dissecting the biochemical and structural determinants of integrin-ligand interactions, particularly those involving the glycoprotein IIb/IIIa (αIIbβ3) receptor. Its unique molecular configuration makes it especially relevant for studies focused on post-translational modifications, peptide-receptor binding dynamics, and structure-activity relationships within the context of platelet biology and thrombosis research.
Integrin Receptor Binding Studies: Deamidated-Eptifibatide serves as a specialized reagent for in vitro investigations of integrin αIIbβ3 binding affinity and selectivity. By introducing a deamidated residue, researchers can systematically compare the binding kinetics and receptor engagement properties relative to its parent compound. This allows for detailed mapping of the molecular determinants governing ligand recognition, informing both fundamental integrin biology and the rational design of next-generation antithrombotic agents.
Platelet Aggregation Assays: In platelet function research, this modified peptide is employed to assess the impact of specific amino acid alterations on the inhibition of platelet aggregation. Its use in turbidimetric or impedance-based aggregation assays enables scientists to evaluate how deamidation influences the efficacy and mechanism of action of cyclic peptides targeting platelet surface receptors. Such studies provide insight into the structural features critical for modulating platelet activity and thrombus formation.
Structure-Activity Relationship (SAR) Analysis: The availability of deamidated analogs like this one facilitates comprehensive SAR studies, allowing researchers to probe the effect of side-chain modifications on peptide stability, bioactivity, and receptor specificity. By comparing biological responses elicited by native and deamidated forms, scientists can delineate the contributions of individual residues to overall peptide function, guiding the optimization of peptide-based ligands for research and development applications.
Peptide Degradation and Post-Translational Modification Research: The deamidated form of eptifibatide is a valuable model for studying spontaneous peptide degradation pathways and the biochemical consequences of deamidation, a common post-translational modification. Researchers utilize it to investigate how such modifications alter peptide conformation, receptor interaction, and biological activity, thereby gaining a deeper understanding of protein and peptide aging, stability, and function in physiological and experimental settings.
Analytical Method Development: In the context of analytical biochemistry, deamidated peptide standards are essential for the development and validation of mass spectrometry-based assays and chromatographic techniques. This compound enables accurate calibration and identification of deamidated species in complex biological samples, supporting advanced proteomic and peptidomic investigations that require precise discrimination between modified and unmodified peptides.
3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
5. Implications of ligand-receptor binding kinetics on GLP-1R signalling
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