H-DL-Pyr-DL-Phe-DL-xiThr-DL-Asp-DL-Val-DL-Asp-DL-Cys(1)-DL-Ser-DL-Val-DL-Ser-DL-Lys-DL-Glu-DL-Cys(2)-DL-Trp-DL-Ser-DL-Val-DL-Cys(3)-DL-Lys-DL-Asp-DL-Leu-DL-Phe-Gly-DL-Val-DL-Asp-DL-Arg-Gly-DL-Lys-DL-Cys(1)-DL-Met-Gly-DL-Lys-DL-Lys-DL-Cys(2)-DL-Arg-DL-Cys(3)-DL-Tyr-DL-Gln-OH.TFA represents a long, mixed-chirality peptide with extensive structural diversity. Functional residues create a wide array of hydrogen-bond possibilities and folding patterns. Researchers examine its domain flexibility and interaction tendencies. Applications include structural biophysics, peptide-material design, and sequence-function analysis.
CAT No: R2686
CAS No:182897-30-9
Synonyms/Alias:H-DL-Pyr-DL-Phe-DL-xiThr-DL-Asp-DL-Val-DL-Asp-DL-Cys(1)-DL-Ser-DL-Val-DL-Ser-DL-Lys-DL-Glu-DL-Cys(2)-DL-Trp-DL-Ser-DL-Val-DL-Cys(3)-DL-Lys-DL-Asp-DL-Leu-DL-Phe-Gly-DL-Val-DL-Asp-DL-Arg-Gly-DL-Lys-DL-Cys(1)-DL-Met-Gly-DL-Lys-DL-Lys-DL-Cys(2)-DL-Arg-DL-Cys(3)-DL-Tyr-DL-Gln-OH.TFA;182897-30-9;H-DL-Pyr-DL-Phe-DL-xiThr-DL-Asp-DL-Val-DL-Asp-DL-Cys(1)-DL-Ser-DL-Val-DL-Ser-DL-Lys-DL-Glu-DL-Cys(2)-DL-Trp-DL-Ser-DL-Val-DL-Cys(3)-DL-Lys-DL-Asp-DL-Leu-DL-Phe-Gly-DL-Val-DL-Asp-DL-Arg-Gly-DL-Lys-DL-Cys(1)-DL-Met-Gly-DL-Lys-DL-Lys-DL-Cys(2)-DL-Arg-DL-Cys(3)-DL-Tyr-DL-Gln-OH.TFA;
H-DL-Pyr-DL-Phe-DL-xiThr-DL-Asp-DL-Val-DL-Asp-DL-Cys(1)-DL-Ser-DL-Val-DL-Ser-DL-Lys-DL-Glu-DL-Cys(2)-DL-Trp-DL-Ser-DL-Val-DL-Cys(3)-DL-Lys-DL-Asp-DL-Leu-DL-Phe-Gly-DL-Val-DL-Asp-DL-Arg-Gly-DL-Lys-DL-Cys(1)-DL-Met-Gly-DL-Lys-DL-Lys-DL-Cys(2)-DL-Arg-DL-Cys(3)-DL-Tyr-DL-Gln-OH.TFA is a complex synthetic peptide featuring a diverse sequence of both D- and L-amino acids, including multiple cysteine residues that can facilitate unique conformational structures. The presence of trifluoroacetic acid (TFA) as a counterion supports its solubility and handling in laboratory settings. This peptide's intricate architecture, which incorporates non-standard residues such as xiThr and multiple sites for potential disulfide bond formation, renders it a versatile molecule for advanced biochemical research. Its design allows for the exploration of structure-activity relationships, folding dynamics, and interactions with various biomolecules, making it an invaluable tool in the realms of peptide chemistry and molecular biology.
Peptide folding and structure-function studies: H-DL-Pyr-DL-Phe-DL-xiThr-DL-Asp-DL-Val-DL-Asp-DL-Cys(1)-DL-Ser-DL-Val-DL-Ser-DL-Lys-DL-Glu-DL-Cys(2)-DL-Trp-DL-Ser-DL-Val-DL-Cys(3)-DL-Lys-DL-Asp-DL-Leu-DL-Phe-Gly-DL-Val-DL-Asp-DL-Arg-Gly-DL-Lys-DL-Cys(1)-DL-Met-Gly-DL-Lys-DL-Lys-DL-Cys(2)-DL-Arg-DL-Cys(3)-DL-Tyr-DL-Gln-OH.TFA is ideally suited for investigating peptide folding mechanisms and the influence of D-amino acids on secondary and tertiary structures. Researchers can utilize this peptide to systematically study how the arrangement of D- and L-amino acids, as well as the strategic positioning of cysteine residues, impacts the formation of disulfide bonds and overall molecular conformation. Such studies provide critical insights into protein engineering, enabling the rational design of peptides and proteins with tailored stability, activity, or resistance to proteolytic degradation.
Disulfide bond engineering and redox biology: The sequence's three distinct cysteine positions offer a robust platform for exploring disulfide bond formation, rearrangement, and reduction-oxidation (redox) processes. By subjecting the peptide to various oxidative or reductive environments, scientists can dissect the kinetics and thermodynamics of disulfide shuffling, which is central to understanding protein maturation, folding diseases, and the development of redox-sensitive biomolecules. These experiments are particularly valuable in the context of designing novel peptide-based scaffolds with enhanced structural rigidity or dynamic redox-switchable functions.
Enzyme substrate and inhibitor development: The unique sequence of this synthetic peptide, which includes non-canonical amino acids and multiple charged residues, makes it an excellent candidate for use as a substrate or competitive inhibitor in enzymology research. It can be employed to probe the specificity and catalytic mechanisms of proteases, peptidases, or other enzymes that recognize or modify peptide substrates. By varying the sequence or introducing site-specific modifications, researchers can map enzyme active sites, elucidate substrate recognition motifs, and develop prototype inhibitors for further optimization.
Biophysical and spectroscopic analysis: This peptide's complex composition and potential for diverse conformational states render it a valuable model for biophysical studies using techniques such as circular dichroism (CD), nuclear magnetic resonance (NMR) spectroscopy, and mass spectrometry. Scientists can leverage the peptide to benchmark and refine analytical methodologies for characterizing secondary structure, disulfide connectivity, and dynamic conformational changes. These applications are essential for advancing the precision of peptide and protein analysis in both academic and industrial laboratories.
Interaction studies and molecular recognition: The amphipathic and multifunctional nature of H-DL-Pyr-DL-Phe-DL-xiThr-DL-Asp-DL-Val-DL-Asp-DL-Cys(1)-DL-Ser-DL-Val-DL-Ser-DL-Lys-DL-Glu-DL-Cys(2)-DL-Trp-DL-Ser-DL-Val-DL-Cys(3)-DL-Lys-DL-Asp-DL-Leu-DL-Phe-Gly-DL-Val-DL-Asp-DL-Arg-Gly-DL-Lys-DL-Cys(1)-DL-Met-Gly-DL-Lys-DL-Lys-DL-Cys(2)-DL-Arg-DL-Cys(3)-DL-Tyr-DL-Gln-OH.TFA supports its use in studies of molecular recognition and binding interactions. Researchers can investigate how the peptide associates with membranes, proteins, or small molecules, providing valuable data for the design of biosensors, affinity tags, or molecular probes. Its sequence diversity enables the modeling of complex interaction networks, contributing to the understanding of biomolecular recognition processes fundamental to cellular signaling, transport, and regulation.
Peptide-based materials and nanotechnology: The structural and chemical versatility of this synthetic peptide makes it an attractive building block for the development of novel peptide-based materials and nanostructures. By exploiting its ability to form defined secondary structures and disulfide-stabilized frameworks, scientists can design self-assembling systems, hydrogels, or nanofibers with tunable properties. These materials have potential utility in areas such as drug delivery, tissue engineering, and the fabrication of responsive biomaterials, where precise control over molecular architecture is essential for function and performance.
1. Cationic cell-penetrating peptides are potent furin inhibitors
2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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