P11 is potent antagonist of the integrin αvβ3-vitronectin interaction (IC50 = 25.72 nM). It can blocks proliferation and induces apoptosis in HUVECs. It exhibits antiangiogenic property.
P11, also known as the peptide sequence corresponding to residues 136-146 of the prion protein, is a synthetic peptide widely utilized in neurodegenerative disease research and protein misfolding studies. As a short peptide fragment derived from the prion protein, P11 is characterized by its relevance to the structural and functional analysis of prion biology. Its sequence is implicated in the conformational changes associated with prion diseases, making it a valuable tool for exploring the molecular mechanisms underlying protein aggregation, amyloid formation, and neurotoxicity. The availability of P11 in a purified, research-grade form enables investigators to probe specific aspects of prion peptide interactions, aggregation pathways, and structure-function relationships with high experimental control.
Protein aggregation research: P11 is extensively employed in studies investigating the mechanisms of protein misfolding and aggregation, particularly in the context of prion diseases such as Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies. Its sequence is known to participate in the formation of β-sheet-rich amyloid fibrils, providing a model system for examining the physicochemical factors that drive peptide self-association. Researchers utilize this peptide to monitor aggregation kinetics, characterize oligomerization intermediates, and elucidate the structural transitions that lead to amyloid fibril formation. These studies contribute to a broader understanding of the molecular basis of neurodegenerative disorders and inform strategies for therapeutic intervention at the aggregation level.
Structural biology and spectroscopy: The defined sequence and aggregation propensity of P11 make it an ideal candidate for structural characterization using techniques such as circular dichroism (CD) spectroscopy, nuclear magnetic resonance (NMR), and X-ray crystallography. By analyzing the conformational preferences of this peptide under various experimental conditions, scientists gain insights into the secondary structure elements that facilitate β-sheet formation and prion-like folding. These structural investigations are essential for mapping the critical determinants of prion protein misfolding and for identifying sequence motifs that govern amyloidogenicity across related peptide systems.
Peptide-membrane interaction studies: The interaction of prion-derived peptides with cellular membranes is believed to play a crucial role in mediating neurotoxicity and facilitating the cellular uptake of misfolded proteins. P11 serves as a model peptide for probing the biophysical and biochemical interactions between amyloidogenic sequences and lipid bilayers. Through fluorescence spectroscopy, calorimetry, and membrane leakage assays, researchers assess how this peptide associates with, inserts into, or disrupts model membranes. These studies are instrumental in clarifying the role of membrane interactions in prion pathogenesis and can support the design of inhibitors that target peptide-lipid interfaces.
Screening of aggregation modulators: In drug discovery and chemical biology, P11 is used as a substrate for screening small molecules, peptides, or antibodies that modulate prion peptide aggregation. Its well-characterized aggregation behavior allows for reproducible in vitro assays to identify compounds that inhibit or alter the kinetics of fibril formation. Such screening platforms are vital for the early-stage evaluation of anti-aggregation agents and for advancing the development of molecular probes or therapeutic leads targeting prion-related disorders.
Analytical method development: The physicochemical properties and aggregation-prone nature of P11 render it a useful reference standard in the development and validation of analytical techniques for detecting amyloidogenic peptides. Researchers utilize it to optimize protocols for high-performance liquid chromatography (HPLC), mass spectrometry, and other analytical platforms aimed at quantifying peptide aggregation, monitoring conformational changes, or characterizing oligomeric species. Employing this peptide in method development ensures robust, sensitive detection of protein misfolding events in both basic and applied research contexts.
p11 alone can associate with the plasma membrane in the absence of ANX2 and facilitate plasmin activation and invasiveness in colorectal cancer cells. Upregulation of p11 has been reported in several cancers including renal cell carcinoma, squamous non-cell lung cancer, anaplastic large cell lymphoma, and pediatric intracranial ependymoma. However, the role of the p11 in the development and progression of acute lymphoblastic leukemia has not been intensely investigated.
Disruption of Annexin II /p11 Interaction Suppresses Leukemia Cell Binding, Homing and Engraftment, and Sensitizes the Leukemia Cells to Chemotherapy
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