H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe includes fluorinated aromatic residues and D-amino acids that alter steric and electronic properties. The sequence enables evaluation of stability, hydrophobic interactions, and folding patterns. Researchers examine its behavior in solution and binding studies. Applications include structural probing, ligand-design research, and conformational analysis.
CAT No: R2516
CAS No:136207-23-3
Synonyms/Alias:BIM-26226;136207-23-3;bim26226;SCHEMBL10005187;HY-P0039;DA-51123;CS-0014927;
H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe is a synthetic peptide featuring a unique sequence that incorporates a pentafluorophenylalanine residue and a C-terminal methyl ester modification. This peptide is designed to enhance stability and modulate biological activity, making it a valuable tool for advanced research applications. Its structure allows for increased resistance to enzymatic degradation, which is particularly beneficial for studies requiring prolonged peptide activity. The inclusion of both D- and L-amino acids, as well as non-standard modifications, provides an opportunity to investigate structure-activity relationships and the effects of side-chain chemistry on peptide behavior. As a result, H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe is frequently selected for use in biochemical, pharmacological, and biophysical research settings where robust and versatile molecular probes are required.
Peptide-Protein Interaction Studies: H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe serves as a specialized probe for exploring peptide-protein interactions due to its enhanced stability and distinctive side-chain features. Researchers can utilize this peptide to map binding sites, assess affinity, and elucidate the molecular mechanisms underlying protein recognition events. Its resistance to proteolytic cleavage ensures that it remains intact during incubation with various protein targets, thereby yielding more reliable and interpretable results in binding assays, co-immunoprecipitation, and pull-down experiments. The presence of the pentafluorophenylalanine residue further enables the study of π-stacking and hydrophobic interactions, providing deeper insight into the forces governing peptide-protein association.
Receptor Binding Assays: The sequence of H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe is designed to facilitate receptor binding studies, particularly in systems where ligand specificity and prolonged activity are essential. By incorporating both D-amino acids and a methyl ester group, this peptide demonstrates increased resistance to metabolic breakdown, allowing it to remain active during extended incubation periods. Scientists can employ it as a ligand analog or competitor in receptor-ligand binding assays to characterize receptor subtypes, profile binding kinetics, and identify novel modulators. Its unique chemical features also make it suitable for use in radioligand displacement experiments, where high stability and specificity are crucial.
Structure-Activity Relationship (SAR) Analysis: The combination of non-standard amino acids and terminal modifications in H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe provides a foundation for detailed SAR studies. Researchers can systematically alter the sequence or functional groups of this peptide to examine the impact on biological activity, binding affinity, and selectivity. Such investigations are instrumental in the rational design of new bioactive peptides with optimized properties for downstream applications. The pentafluorophenylalanine residue, in particular, offers a point of comparison with standard phenylalanine, enabling the exploration of electronic and steric effects on peptide function.
Fluorescence and Spectroscopic Probing: The inclusion of tryptophan in the sequence of H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe makes it an excellent candidate for fluorescence-based studies. Researchers can exploit the intrinsic fluorescence of tryptophan to monitor peptide conformational changes, folding dynamics, and interactions with other biomolecules. Additionally, the unique side-chain chemistry of the pentafluorophenylalanine residue may be leveraged in spectroscopic analyses, such as NMR or mass spectrometry, to gain further structural and environmental information. These features make the peptide a valuable tool for investigating molecular mechanisms at high resolution.
Enzyme Substrate and Inhibitor Studies: H-D-Phe(F5)-Gln-Trp-Ala-Val-D-Ala-His-Leu-OMe is also utilized in the study of enzyme specificity and inhibition. Its modified sequence can serve as a substrate analog for proteases, allowing researchers to probe enzyme active sites and determine substrate preferences. The peptide's resistance to enzymatic cleavage makes it suitable for competitive inhibition studies, where it can be used to assess the potency and selectivity of enzyme inhibitors. By enabling the dissection of enzyme mechanisms and substrate recognition, this peptide supports the development of novel modulators and enhances our understanding of enzymology.
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