G3-C12 (TFA) is a galectin-3 binding peptide, with Kd of 88 nM, and shows anticancer activity.
CAT No: R1368
G3-C12 TFA, also known as Gly-Gly-Gly-dodecanoic acid trifluoroacetate salt, is a synthetic peptide conjugate featuring a tripeptide backbone (glycyl-glycyl-glycine) N-terminally modified with a lauric acid (dodecanoic acid) moiety. This amphiphilic structure combines the hydrophilic properties of a peptide with the hydrophobic characteristics of a medium-chain fatty acid, making it an important tool for probing peptide-lipid interactions and studying membrane-associated processes. Its unique configuration facilitates research in peptide self-assembly, membrane mimicry, and the development of novel biomaterials, providing valuable insights into the interface between peptide chemistry and lipid biology.
Peptide-membrane interaction studies: G3-C12 TFA is widely employed in investigations of peptide-lipid interactions due to its amphiphilic nature. The lauric acid tail enables the peptide to insert into or associate with lipid bilayers, serving as a model for understanding how lipidated peptides interact with biological membranes. Researchers utilize this compound to elucidate mechanisms of membrane anchoring, partitioning, and perturbation, which are relevant to both fundamental biochemistry and the design of membrane-active peptides.
Amphiphilic self-assembly research: The conjugation of a hydrophobic fatty acid to a hydrophilic peptide sequence enables G3-C12 TFA to participate in self-assembly processes, forming micelles, vesicles, or nanostructures in aqueous environments. This property is leveraged in studies exploring the rules governing peptide-driven self-assembly, with applications in the design of supramolecular biomaterials, nanocarriers, and responsive delivery systems. Its predictable self-assembly behavior serves as a model for constructing peptide-based nanostructures with tunable properties.
Peptide synthesis and modification studies: As a representative of lipidated peptides, G3-C12 TFA is valuable in synthetic peptide chemistry for method development and optimization. Researchers use it to assess strategies for the incorporation of fatty acid chains into peptide backbones, evaluate coupling efficiencies, and study the effects of lipidation on peptide solubility and purification. These investigations support the advancement of synthetic protocols for generating a wide range of lipopeptide derivatives.
Biophysical characterization and analytical method development: The well-defined structure of G3-C12 TFA makes it a suitable standard or probe in analytical techniques such as mass spectrometry, high-performance liquid chromatography, and circular dichroism spectroscopy. Its amphiphilic character challenges and informs the development of separation and detection methods for lipopeptides, aiding in the refinement of protocols for the characterization of complex peptide-lipid conjugates.
Model system for membrane protein anchoring: G3-C12 TFA can serve as a surrogate for natural lipid-modified peptides in studies aimed at understanding protein localization and anchoring to cellular membranes. By mimicking the lipidation found in certain signaling peptides and proteins, it allows researchers to dissect the physicochemical parameters that govern membrane association, lateral mobility, and partitioning within lipid domains, providing a controlled system for dissecting the role of lipid modifications in protein-membrane interactions.
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