LPYFD-NH2 is a neuroprotective peptide that binds to amyloid beta (Aβ) and protects neurons against toxic effects of Aβ (1-42) in vitro and in vivo.
CAT No: R0821
CAS No:700361-48-4
Synonyms/Alias:LPYFD-NH2;700361-48-4;LPYFD;(3S)-4-amino-3-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-amino-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-phenylpropanoyl]amino]-4-oxobutanoic acid;Leu-Pro-Tyr-Phe-Asp amide;Leu-Pro-Tyr-Phe-Asp-amide;HY-P1060;AKOS024457970;PD070349;CS-0026093;(S)-4-Amino-3-((S)-2-((S)-2-((S)-1-((S)-2-amino-4-methylpentanoyl)pyrrolidine-2-carboxamido)-3-(4-hydroxyphenyl)propanamido)-3-phenylpropanamido)-4-oxobutanoic acid;
LPYFD-NH2 is a synthetic peptide corresponding to the C-terminal pentapeptide fragment of the human lipoprotein lipase inhibitor, often studied for its role in modulating protein-protein interactions and cellular signaling pathways. As a custom-designed peptide, it features an amidated C-terminus, which enhances its stability and bioactivity in experimental settings. Researchers utilize this sequence to probe the structure-activity relationships of peptide-based inhibitors and to investigate mechanisms underlying lipid metabolism, enzyme regulation, and molecular recognition. Its defined sequence and modifiable termini make it a valuable tool for a range of biochemical and molecular biology applications, supporting advanced research in peptide function and interaction studies.
Peptide-protein interaction studies: LPYFD-NH2 is frequently employed in investigations of peptide-mediated modulation of protein interactions, particularly involving enzymes such as lipoprotein lipase and related regulatory proteins. By serving as a model ligand or inhibitor, the peptide allows researchers to dissect the molecular determinants of binding affinity and specificity. This application is critical for elucidating the mechanistic basis of enzyme regulation, providing insights into how short peptide sequences can influence complex biochemical pathways.
Enzyme inhibition assays: The pentapeptide is widely used in enzyme inhibition assays to characterize its capacity to modulate lipase activity or to serve as a prototype for designing novel inhibitory peptides. Its defined sequence permits systematic structure-activity relationship analysis, enabling the identification of key residues responsible for inhibitory potency. Through such assays, scientists can evaluate the functional consequences of peptide modification, contributing to the development of targeted biochemical tools for lipid metabolism research.
Peptide structure-activity relationship (SAR) analysis: LPYFD-NH2 is a valuable template for SAR studies, where systematic modifications to its amino acid sequence or terminal groups are evaluated for their impact on biological activity. Researchers utilize these studies to map critical functional motifs within the peptide, advancing understanding of how sequence alterations affect molecular recognition and stability. This knowledge underpins the rational design of more effective peptide analogs for experimental and industrial use.
Cell signaling and receptor binding research: As a defined bioactive peptide, LPYFD-NH2 is instrumental in exploring cellular signaling mechanisms and receptor-ligand interactions. By introducing the peptide into cell-based assays, investigators can monitor downstream signaling events, assess receptor specificity, and delineate pathways influenced by peptide engagement. Such studies are essential for mapping cellular responses to peptide stimuli and for identifying potential modulators of metabolic or regulatory pathways.
Peptide synthesis and analytical validation: The sequence and amidated terminus of LPYFD-NH2 make it a useful standard for optimizing solid-phase peptide synthesis protocols and validating analytical methods such as HPLC and mass spectrometry. Researchers and technical laboratories employ the peptide to calibrate instrumentation, refine purification strategies, and establish quality control benchmarks for custom peptide production. Its consistent performance in analytical workflows supports reproducibility and reliability in peptide research and manufacturing environments.
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