Kspwfttl incorporates aromatic, hydrophobic, and polar residues that influence secondary-structure preference. The compact sequence supports exploration of side-chain packing in β-turn and loop motifs. Researchers investigate its behavior to understand sequence-dependent folding. Applications include peptide-material design, motif stabilization studies, and bioorganic interaction analysis.
CAT No: R2294
CAS No:153049-05-9
Synonyms/Alias:KSPWFTTL;153049-05-9;HY-P3333;AKOS040756880;DA-54693;CS-0311776;(2S)-2-[[(2S,3R)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carbonyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxybutanoyl]amino]-4-methylpentanoic acid;
Kspwfttl is a synthetic peptide compound engineered for specialized research applications in the fields of peptide science, molecular biology, and biochemical analysis. As a defined sequence peptide, it offers a valuable tool for studies focused on protein-protein interactions, receptor binding, and the elucidation of signaling pathways. Its precise amino acid arrangement allows researchers to investigate sequence-specific functions, structure-activity relationships, and the underlying mechanisms of peptide-mediated processes. The compound's stability and reproducibility make it an ideal candidate for both exploratory research and more targeted experimental designs seeking to understand the role of short peptides in biological systems.
Peptide functional studies: In experimental settings, Kspwfttl is frequently employed to probe the functional significance of specific peptide motifs within larger protein frameworks. By introducing this sequence into in vitro assays, researchers can assess its influence on cellular signaling, enzymatic activity, or molecular recognition events. Its defined composition enables the dissection of sequence-dependent effects, providing insight into how subtle changes in peptide structure can modulate biological outcomes.
Receptor binding assays: The compound serves as a model ligand in receptor binding studies, enabling the quantification and characterization of peptide-receptor interactions. Through competitive binding experiments and affinity measurements, scientists can determine the specificity, kinetics, and thermodynamics of its association with target receptors. Such data are instrumental in mapping binding sites, validating computational predictions, and guiding the rational design of receptor modulators.
Peptide synthesis optimization: Kspwfttl is also utilized as a benchmark sequence in the development and optimization of peptide synthesis protocols. Its incorporation into synthetic workflows allows chemists to evaluate the efficiency of coupling reagents, assess the fidelity of solid-phase synthesis techniques, and troubleshoot sequence-specific synthesis challenges. This application supports the advancement of peptide manufacturing technologies and enhances the reliability of custom peptide production.
Analytical method development: The defined structure and physicochemical properties of this peptide make it a suitable standard for the calibration and validation of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. By serving as a reference compound, it assists in the establishment of detection limits, quantification protocols, and method robustness, thereby ensuring the accuracy and reproducibility of peptide analysis in complex biological samples.
Structure-activity relationship (SAR) investigations: Researchers leverage Kspwfttl in SAR studies to systematically explore how modifications to its sequence or chemical structure affect biological activity. By synthesizing and testing analogs with targeted substitutions, scientists can pinpoint critical residues responsible for activity, binding, or stability. Such investigations are foundational for the rational design of novel bioactive peptides, peptidomimetics, and therapeutic candidates, contributing to the broader understanding of peptide-based molecular recognition and function.
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