ATWLPPR Peptide assembles aromatic, hydrophobic, and basic residues that influence local folding and ligand recognition. The sequence supports exploration of β-turn formation and receptor-binding determinants. Researchers evaluate its interactions in aqueous and membrane-mimetic systems. Use spans peptide-based probe design, structural modeling, and bioorganic interaction studies.
CAT No: R2298
CAS No:272121-15-0
Synonyms/Alias:ATWLPPR Peptide;CHEMBL1095672;272121-15-0;Ala-Thr-Trp-Leu-Pro-Pro-Arg;ATWLPPR;HY-P1663;BDBM50317441;CS-0084563;(2S)-2-[[(2S)-1-[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-aminopropanoyl]amino]-3-hydroxybutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic acid;
ATWLPPR Peptide is a synthetic heptapeptide widely recognized for its role as a selective antagonist of neuropilin-1 (NRP-1), a key co-receptor involved in vascular endothelial growth factor (VEGF) signaling. By mimicking the C-terminal sequence of VEGF165, this peptide exhibits a high affinity for the NRP-1 binding site, thereby modulating critical pathways associated with angiogenesis, vascular permeability, and cellular migration. Its well-characterized biochemical properties and specificity have positioned it as a valuable research tool for dissecting molecular mechanisms underlying vascular biology and neurobiology. The sequence and structure of ATWLPPR Peptide enable precise interaction studies, making it a foundational resource for investigations into the modulation of VEGF-mediated processes.
Angiogenesis research: As a competitive inhibitor of VEGF165 binding to NRP-1, ATWLPPR Peptide is extensively utilized in studies exploring the regulation of new blood vessel formation. By selectively blocking the VEGF-NRP-1 interaction, the peptide allows researchers to delineate the contribution of NRP-1 to endothelial cell proliferation, migration, and tube formation. Its application in in vitro and ex vivo angiogenesis models provides critical insights into the molecular drivers of neovascularization, supporting the identification of novel anti-angiogenic strategies for basic science and preclinical research.
Signal transduction studies: The peptide's ability to interfere with VEGF-NRP-1 signaling has made it a preferred probe in the analysis of downstream signaling cascades. By disrupting complex formation between NRP-1 and VEGF receptors, ATWLPPR enables detailed investigation of intracellular pathways such as PI3K/Akt, MAPK/ERK, and focal adhesion kinase (FAK) signaling. These studies are essential for understanding how NRP-1 modulates cellular responses to growth factors, and for clarifying the broader implications of NRP-1 signaling in various physiological and pathological contexts.
Neurobiology research: Beyond its vascular applications, the peptide is also employed to probe the role of NRP-1 in neural development and axonal guidance. NRP-1 is a well-established receptor for class 3 semaphorins, which are crucial for neuronal patterning. By acting as a molecular tool to inhibit NRP-1 ligand interactions, ATWLPPR facilitates studies aimed at elucidating the mechanisms governing neural cell migration, differentiation, and synaptic connectivity. Such research is vital for advancing the understanding of neurodevelopmental processes and their dysregulation.
Vascular permeability assays: Due to its specificity for NRP-1, the peptide is frequently used in experimental systems designed to assess changes in endothelial barrier function. By modulating the VEGF-NRP-1 axis, it enables researchers to quantify alterations in vascular permeability under various experimental conditions. These assays are instrumental in exploring the molecular determinants of vascular leakage, which has implications for inflammation, tissue repair, and the pathophysiology of edema.
Peptide-based inhibitor validation: As a model peptide inhibitor, ATWLPPR is often incorporated into studies that compare the efficacy and selectivity of novel NRP-1 antagonists. Its well-characterized interaction profile serves as a benchmark in competitive binding assays, functional cell-based experiments, and structure-activity relationship (SAR) analyses. The use of this peptide in validation workflows supports the development of next-generation peptide therapeutics and research probes targeting the VEGF-NRP-1 axis.
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