Phytochelatin 2 (PC2) (TFA) consists of γ-glutamyl-cysteine repeats terminating in glycine, forming a metal-binding thiol-rich peptide. The structure supports studies of metal chelation, redox behavior, and folding transitions. Researchers examine its conformational flexibility and coordination geometry. Its TFA form provides consistent analytical purity.
CAT No: R2226
CAS No:1426828-27-4
Synonyms/Alias:Phytochelatin 2 (PC2) (TFA);HY-P2512A;1426828-27-4;CS-0904965;
Phytochelatin 2 (PC2) (TFA) is a synthetic peptide derivative composed of repeating γ-glutamylcysteine units followed by a terminal glycine, reflecting the core structure of naturally occurring phytochelatins. As a member of the phytochelatin family, PC2 is notable for its high affinity for binding heavy metal ions through its cysteine thiol groups, playing a crucial role in metal detoxification and homeostasis in plants and other organisms. The trifluoroacetic acid (TFA) salt form enhances its solubility and stability for laboratory applications. Due to its unique biochemical properties, PC2 is widely studied in the context of plant biochemistry, environmental toxicology, and analytical chemistry, serving as a valuable tool for elucidating mechanisms of metal chelation and stress response.
Metal chelation studies: PC2 serves as an essential model compound for investigating the molecular mechanisms underlying heavy metal ion sequestration in biological systems. Its well-defined structure allows researchers to study the stoichiometry, kinetics, and thermodynamics of metal-peptide interactions, particularly with cadmium, lead, arsenic, and mercury. These studies are fundamental for understanding how plants and some microorganisms mitigate metal toxicity, as well as for the development of biosensors and bioremediation strategies.
Environmental toxicology research: The peptide is frequently employed in experiments aimed at elucidating the roles of phytochelatins in environmental stress adaptation. By incorporating PC2 into in vitro and in vivo assays, scientists can simulate and analyze plant responses to heavy metal exposure, thereby gaining insights into the regulation of metal uptake, transport, and compartmentalization. Such research supports the identification of biomarkers for environmental monitoring and the assessment of ecological risks associated with metal contamination.
Analytical method development: PC2 is used as a reference standard and calibration compound in advanced analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its defined sequence and reactivity make it ideal for method validation, quantification of phytochelatins in complex biological samples, and optimization of detection protocols for thiol-containing peptides. This enables more accurate profiling of metal-peptide complexes in plant tissues and environmental matrices.
Peptide synthesis validation: The synthetic production of PC2 provides a benchmark for evaluating peptide synthesis methodologies, particularly those involving the assembly of γ-glutamylcysteine motifs. Researchers utilize it to test coupling efficiency, peptide purification strategies, and post-synthetic modifications relevant to thiol-rich peptides. These validation studies are critical for advancing solid-phase peptide synthesis technologies and for generating structurally precise analogs for further biochemical exploration.
Structural and functional studies: PC2 is instrumental in biophysical and structural investigations aimed at deciphering the conformational dynamics of metal-binding peptides. Techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and X-ray crystallography are employed to characterize its three-dimensional structure and to map the spatial arrangement of thiol groups upon metal coordination. The resulting data enhance our understanding of the structural determinants of metal selectivity and affinity, informing the design of synthetic chelators and metal-responsive biomolecules.
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