Peptide C105Y

Peptide C105Y, a synthetic and cell-penetrating peptide based on the amino acid sequence corresponding to residues 359-374 of α1-antitrypsin, enhances gene expression from DNA nanoparticles.

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

CAT No: R1608

CAS No:247572-63-0

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cGMP Peptide
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M.F/Formula
C₉₇H₁₄₈N₂₀O₂₃S
M.W/Mr.
1994.40
Sequence
One Letter Code: CSIPPEVKFNKPFVYLI
three Letter Code: Cys-Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile

Peptide C105Y is a synthetic peptide compound characterized by a specific amino acid sequence that imparts unique biochemical properties, making it a valuable tool in peptide research and functional studies. As a member of the peptide class, C105Y is designed to facilitate investigations into protein-protein interactions, molecular recognition events, and the modulation of biological pathways. Its defined structure and sequence specificity enable researchers to probe mechanistic aspects of peptide function and advance the understanding of biomolecular systems. Owing to its versatility, Peptide C105Y is frequently employed in diverse experimental contexts within the fields of molecular biology, biochemistry, and biomedical research.

Peptide-based interaction studies: In the context of protein-protein interaction research, C105Y serves as a model system for elucidating the principles of molecular recognition and binding specificity. By incorporating this peptide into binding assays or pull-down experiments, scientists can dissect the determinants of affinity and selectivity between peptides and their target proteins. Such studies contribute to mapping interaction domains, characterizing binding interfaces, and identifying critical residues involved in complex formation, thus enhancing the broader understanding of cellular signaling networks and regulatory mechanisms.

Structure-activity relationship (SAR) analysis: The defined sequence of C105Y allows for systematic exploration of structure-activity relationships in peptide biology. Researchers can introduce targeted modifications, such as amino acid substitutions or chemical labeling, to assess the impact on biological activity, stability, or receptor binding. These SAR investigations are essential for optimizing peptide function, evaluating analogs, and guiding the rational design of improved peptide-based probes or modulators. Insights gained from such studies inform both basic research and the development of novel peptide technologies.

Peptide synthesis and method validation: C105Y is frequently utilized as a reference or test substrate in the optimization and validation of solid-phase peptide synthesis protocols. Its sequence complexity and physicochemical properties provide an effective benchmark for assessing coupling efficiency, purification methodologies, and analytical techniques such as HPLC or mass spectrometry. Employing this peptide in methodological workflows enables laboratories to ensure reproducibility, troubleshoot synthetic challenges, and refine process parameters for the generation of high-quality custom peptides.

Biochemical assay development: The unique characteristics of C105Y make it suitable for incorporation into a variety of biochemical assays, including enzyme kinetics, receptor binding, and competitive inhibition studies. By serving as a substrate, ligand, or competitor, the peptide enables the quantitative evaluation of enzymatic activity, binding affinities, or inhibitor potency. Its use in assay development supports the creation of robust analytical platforms for screening, mechanistic elucidation, or functional characterization of biomolecular interactions.

Cellular uptake and localization studies: Due to its customizable sequence and modifiable termini, C105Y is also employed in investigations of peptide cell permeability and intracellular trafficking. Researchers utilize this peptide to study uptake mechanisms, endocytic pathways, and subcellular localization by conjugating it with fluorescent tags or other reporter groups. These studies provide valuable information on the determinants of peptide transport, inform the design of cell-penetrating peptides, and facilitate the development of delivery systems for research applications.

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