SW2_110A is a rationally designed peptide variant tuned to interrogate a specific protein surface or signaling domain. Substitutions control hydrophobic packing, charge distribution, and secondary-structure propensity. Researchers use it in binding assays and structural analyses to refine interaction models. Applications include PPI mapping, peptide-optimization projects, and mechanistic biochemistry.
CAT No: R2777
Synonyms/Alias:SW2_110A; 2566738-95-0; MS-31354; HY-141716; Unk-Gly(cPent)-D-aIle-Lys(Et2)-Ser-Unk; CS-0201421; G18313; 2579696-95-8; N-[(1S)-1-cyclopentyl-2-[[(2R,3S)-1-[[(2S)-6-(diethylamino)-1-[[(2S)-3-hydroxy-1-oxo-1-(prop-2-ynylamino)propan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]-4-phenoxybenzamide
SW2_110A is a synthetic peptide compound designed for advanced research applications in molecular biology, signal transduction, and protein-protein interaction studies. As a structurally defined peptide, it serves as a valuable tool for probing cellular mechanisms, particularly those involving regulatory pathways governed by peptide-mediated signaling. Its sequence and conformation are tailored to facilitate specific binding events, making it highly relevant for researchers investigating the intricacies of cellular communication, receptor modulation, and downstream biological responses. The compound's synthetic origin ensures precise control over its molecular properties, supporting reproducible experimentation in both academic and industrial laboratories.
Peptide signaling pathway analysis: SW2_110A is frequently employed in the elucidation of peptide-dependent signaling cascades within cellular systems. By serving as a modulator or mimic of endogenous peptide ligands, it enables researchers to dissect the roles of specific peptide-receptor interactions in cell signaling networks. This application is particularly valuable for mapping out the molecular underpinnings of signal transduction events, including phosphorylation cycles, second messenger production, and gene expression regulation, ultimately advancing the understanding of complex biological processes.
Protein-protein interaction studies: As a structurally defined peptide, SW2_110A is instrumental in characterizing the binding affinities and specificities between proteins and their peptide partners. Its utility extends to competitive binding assays, affinity purification protocols, and surface plasmon resonance experiments, where it can be used to quantify interaction strengths or to identify novel binding domains. Such studies are critical for unraveling the molecular determinants of protein networks, informing the design of inhibitors or modulators with potential research applications.
Peptide synthesis and method development: The compound serves as a reference or model substrate in peptide synthesis workflows, allowing chemists to optimize coupling strategies, purification techniques, and analytical methods. Its well-defined sequence and physicochemical properties make it an ideal candidate for benchmarking solid-phase peptide synthesis protocols, validating chromatographic separation methods, and calibrating mass spectrometric analyses. These applications are essential for ensuring reproducibility and quality in peptide production pipelines.
Cellular functional assays: SW2_110A is utilized in a variety of cell-based functional assays to investigate the biological activity of peptides in vitro. By introducing it into cultured cells, researchers can monitor downstream effects such as alterations in cell viability, proliferation, or differentiation, depending on the biological context. Such assays facilitate the identification of peptide-mediated cellular responses, contributing to a deeper understanding of their roles in physiological and pathological processes.
Structural biology and conformational analysis: The defined sequence and structure of SW2_110A make it suitable for studies aimed at elucidating peptide conformations and dynamics. Techniques such as nuclear magnetic resonance spectroscopy, circular dichroism, and X-ray crystallography can be applied to the compound to gain insights into its secondary and tertiary structure. These investigations are fundamental for correlating structural features with biological activity, guiding the rational design of novel peptides with improved functional characteristics.
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