Pal-Gly-His-Kys-OH trifluoroacetate features a palmitoylated motif that enables evaluation of lipid-peptide conjugation. Glycine, histidine, and lysine contribute flexibility, metal-binding potential, and charge variability. The amphiphilic design aids studies of membrane association and signaling. Research uses include cosmetic peptide modeling, carrier-peptide development, and biophysical interaction analysis.
CAT No: R2204
CAS No:2803375-47-3
Synonyms/Alias:Pal-Gly-His-Lys-OH trifluoroacetate;2803375-47-3;F76498;(2S)-6-amino-2-[[(2S)-2-[[2-(hexadecanoylamino)acetyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]hexanoic acid;2,2,2-trifluoroacetic acid;
Pal-Gly-His-Lys-OH trifluoroacetate is a synthetic peptide derivative recognized for its unique sequence and functional versatility in biochemical research. Composed of palmitoyl-modified glycine, histidine, and lysine residues, this compound exhibits amphiphilic properties and is often utilized as a model peptide in studies involving peptide-membrane interactions, signal transduction, and peptide-based delivery systems. The presence of the palmitoyl group enhances its membrane affinity, making it a valuable tool for investigating lipid-peptide conjugates and their biological behaviors. As a research-use peptide, it serves as a critical component in the exploration of peptide structure-function relationships and the development of novel peptide-based biomaterials.
Peptide-membrane interaction studies: Palmitoylated peptides such as Pal-Gly-His-Lys-OH trifluoroacetate are extensively employed in research focused on understanding the dynamics of peptide association with lipid bilayers. The lipophilic palmitoyl chain facilitates integration into model membranes, enabling detailed analysis of membrane anchoring, peptide orientation, and the influence of lipid modifications on peptide function. Such studies provide valuable insights into cellular signaling mechanisms, membrane protein mimicry, and the design of membrane-active agents.
Signal transduction research: The specific sequence of Gly-His-Lys, when modified by palmitoylation, offers a platform for dissecting the role of post-translational lipidation in cellular signaling pathways. Researchers utilize this peptide to model the effects of lipid modifications on peptide-mediated signaling events, protein-protein interactions, and intracellular localization. Its application in these studies aids in elucidating the functional consequences of lipidation in regulatory proteins and signaling peptides.
Peptide delivery system development: Due to its amphiphilic character, Pal-Gly-His-Lys-OH trifluoroacetate is investigated as a component in the design of peptide-based delivery vehicles. The palmitoyl group confers enhanced membrane permeability, making it suitable for probing peptide transport across biological barriers and optimizing the delivery of bioactive molecules. Experimental systems employing this peptide facilitate the assessment of conjugate stability, cellular uptake, and the potential for targeted delivery applications in vitro.
Structure-activity relationship analysis: The modular nature of this peptide allows for systematic investigation of how sequence modifications and lipid conjugation affect biological activity. Researchers employ Pal-Gly-His-Lys-OH trifluoroacetate in comparative studies to delineate the contributions of palmitoylation, individual amino acid residues, and overall conformation to peptide function. These insights are instrumental in guiding rational design strategies for synthetic peptides with tailored properties.
Analytical method development: The well-defined structure and physicochemical properties of Pal-Gly-His-Lys-OH trifluoroacetate render it a useful standard in the calibration and validation of peptide analysis techniques. Mass spectrometry, high-performance liquid chromatography, and other analytical platforms benefit from the inclusion of such peptides in method optimization, sensitivity assessment, and quality control processes. Its application in these contexts supports robust and reproducible peptide analytics in research and development laboratories.
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