[L-Ala2]-Etelcalcetide substitutes alanine at position 2, modifying steric constraints and backbone geometry. The peptide's thiol and disulfide characteristics remain central to its folding and interaction profile. Researchers investigate structural changes and reactivity patterns. Applications include analog comparison, impurity identification, and structure-function analysis.
CAT No: Z10-101-233
Synonyms/Alias:S-(((S)-2-acetamido-3-(((S)-1-(((R)-1-(((R)-1-(((R)-1-(((R)-1-(((R)-1-amino-5-guanidino-1-oxopentan-2-yl)amino)-1-oxopropan-2-yl)amino)-5-guanidino-1-oxopentan-2-yl)amino)-5-guanidino-1-oxopentan-2-yl)amino)-5-guanidino-1-oxopentan-2-yl)amino)-1-oxopropan-2-yl)amino)-3-oxopropyl)thio)-L-cysteine; Etelcalcetide impurity 2; 2-L-Ala-Etelcalcetide
L-Ala2-Etelcalcetide is a synthetic peptide analog characterized by the substitution of the second amino acid residue with L-alanine in the etelcalcetide sequence. As a modified peptide, it holds significant interest for researchers investigating structure-activity relationships, peptide engineering, and calcium-sensing receptor (CaSR) modulation. The presence of the L-Ala2 substitution provides a unique biochemical tool for dissecting the impact of specific residue changes on peptide conformation, receptor interaction, and downstream signaling. Its tailored structure makes it a valuable resource for both fundamental peptide research and applied studies within the field of receptor pharmacology.
Peptide structure-activity relationship studies: The L-Ala2 variant is frequently utilized in systematic investigations aimed at elucidating how single-residue modifications influence the biological properties of peptide ligands. By comparing the activity and binding affinity of this analog to that of the parent etelcalcetide sequence, researchers can gain insight into the critical determinants of CaSR engagement and activation. Such studies are foundational for advancing the rational design of next-generation peptide modulators with optimized efficacy, selectivity, or stability.
Receptor-ligand interaction analysis: In vitro assays employing this analog enable detailed exploration of peptide-receptor dynamics, particularly with respect to the calcium-sensing receptor. The strategic alanine substitution at position two allows for the assessment of side-chain contributions to binding orientation and interaction energy. These experiments support the mapping of peptide binding sites and the refinement of computational models that predict receptor-ligand behavior, facilitating a deeper understanding of molecular recognition processes.
Peptide engineering and optimization: The L-Ala2 modification serves as a model system for evaluating the effects of targeted amino acid substitutions on peptide stability, folding, and resistance to proteolytic degradation. Incorporating this analog into comparative studies helps identify sequence features that enhance peptide robustness, inform the development of more durable bioactive peptides, and support the optimization of synthetic protocols for peptide-based research reagents.
Analytical method development: The distinct physicochemical properties introduced by the L-alanine substitution make [L-Ala2]-Etelcalcetide a useful standard or reference material for analytical method validation. It can be employed in chromatographic, spectrometric, or electrophoretic techniques to assess separation efficiency, detection sensitivity, and peptide quantification accuracy. Such applications are essential for ensuring the reliability and reproducibility of analytical workflows in peptide-focused laboratories.
Peptide conjugation and labeling studies: The presence of a defined sequence modification offers opportunities for site-specific conjugation or labeling experiments. Researchers may use this analog to explore the impact of chemical modifications on peptide function, investigate labeling strategies for imaging or tracking, or develop tailored peptide conjugates for specialized research applications. These studies contribute to the broader field of peptide functionalization and the creation of versatile research tools for molecular and cellular investigations.
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