Phe-Met-Arg-Phe Like Peptide, Snail Helix aspersa is a FMRF-like peptide from visceral and somatic muscles of the snail Helix aspersa. FMRF (Phe-Met-Arg-Phe) is a neuropeptide peptide consisting of 4 amino acid residues.
CAT No: R1617
CAS No:98495-35-3
Synonyms/Alias:Pqdpflrfamide;98495-35-3;Pyr-Asp-Pro-Phe-Leu-Arg-Phe-NH2;Phe-Met-Arg-Phe Like Peptide, Snail Helix aspersa;FMRF-LIKE PEPTIDE;Pglu-asp-pro-phe-leu-arg-phenh2;(3S)-4-[(2S)-2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-4-oxo-3-[[(2S)-5-oxopyrrolidine-2-carbonyl]amino]butanoic acid;Pyroglutamyl-aspartyl-prolyl-phenylalanyl-leucyl-arginyl-phenylalaninamide;L-Phenylalaninamide, 5-oxo-L-prolyl-L-alpha-aspartyl-L-prolyl-L-phenylalanyl-L-leucyl-L-arginyl-;pGlu-Asp-Pro-Phe-Leu-Arg-Phe-NH2;CHEMBL1415934;HY-P1904;p-Glu-Asp-Pro-Phe-Leu-Arg-Phe-NH2;pyroGlu-Asp-Pro-Phe-Leu-Arg-Phe-NH2;NCGC00167277-01;DA-77250;FP110406;MS-31688;PD197392;CS-0097994;G12239;
Phe-Met-Arg-Phe Like Peptide, Snail Helix aspersa is a synthetic peptide analog inspired by sequences found in the Helix aspersa snail. As a short-chain peptide, it is characterized by its defined sequence of amino acids—phenylalanine, methionine, arginine, and phenylalanine—arranged in a motif that mimics naturally occurring bioactive peptides in gastropods. This compound is of significant interest in biochemical and physiological research due to its structural similarity to endogenous signaling peptides, making it a valuable tool for probing peptide-receptor interactions, studying neuromodulation, and exploring invertebrate peptide function. Its defined sequence and origin provide a unique platform for understanding peptide-mediated processes in molluscan systems and beyond.
Peptide signaling research: The synthetic analog is frequently employed in studies investigating peptide-based signaling pathways in invertebrates. Its sequence, reminiscent of neuropeptides found in mollusks, enables researchers to dissect the molecular mechanisms underlying neurotransmission and neuromodulation. By applying this peptide in vitro or in ex vivo tissue assays, scientists can examine receptor specificity, ligand binding affinity, and downstream signaling events, thereby elucidating the functional roles of related endogenous peptides in Helix aspersa and other gastropods.
Receptor-ligand interaction studies: Due to its defined amino acid sequence, the peptide serves as a model ligand for characterizing the binding properties and activation profiles of peptide receptors. Researchers utilize it to map receptor binding domains, assess structure-activity relationships, and evaluate the effects of sequence modifications on biological activity. These studies provide critical insights into the molecular recognition mechanisms that govern peptide-receptor interactions in both invertebrate and comparative vertebrate systems.
Peptide synthesis validation: The compound is also valuable as a reference standard in synthetic peptide production workflows. Its well-characterized sequence allows for the calibration and optimization of solid-phase peptide synthesis protocols, as well as for the validation of purification and analytical techniques such as HPLC and mass spectrometry. By serving as a benchmark, it ensures the reliability and reproducibility of peptide synthesis, which is essential for downstream biochemical and pharmacological investigations.
Neuropeptide function exploration: In neurobiology, this peptide is utilized to probe the physiological effects of molluscan neuropeptides. Application in isolated ganglia or neural tissue preparations enables the study of electrophysiological responses, synaptic modulation, and behavioral outcomes associated with peptide application. Such experiments advance the understanding of neuromodulatory roles in gastropods and contribute to broader comparative analyses of nervous system evolution and function.
Comparative biochemistry studies: The unique origin and structure of the peptide make it an excellent candidate for comparative studies across species. By analyzing its activity and receptor interactions in different model organisms, researchers can investigate the conservation and divergence of peptide signaling systems. These comparative approaches shed light on evolutionary adaptations and inform the development of bioactive peptides with tailored properties for research and industrial applications.
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