Aip I features a compact peptide motif enriched with hydrophobic and polar residues that shape its conformational behavior. Researchers evaluate its folding dynamics to understand sequence-dependent interactions. Its structural profile supports modeling of receptor-binding determinants. Applications include structural biology, peptide engineering, and motif-function analysis.
CAT No: R2335
CAS No:200010-29-3
Synonyms/Alias:Autoinducing Peptide I;AIP I;200010-29-3;CHEMBL2337554;Autoinducing Peptide I trifluoroacetate salt;2-((3S,6S,9S,12S,15R)-15-(((2S,3R)-2-(((2S)-2-(((2S)-2-amino-3-(4-hydroxyphenyl)propanoyl)amino)-3-hydroxypropanoyl)amino)-3-hydroxybutanoyl)amino)-9-benzyl-6-((2S)-butan-2-yl)-3-(2-methylsulfanylethyl)-2,5,8,11,14-pentaoxo-1-thia-4,7,10,13-tetrazacyclohexadec-12-yl)acetic acid;2-[(3S,6S,9S,12S,15R)-15-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxybutanoyl]amino]-9-benzyl-6-[(2S)-butan-2-yl]-3-(2-methylsulfanylethyl)-2,5,8,11,14-pentaoxo-1-thia-4,7,10,13-tetrazacyclohexadec-12-yl]acetic acid;Staphylococcus aureus AIP-I;CHEBI:216866;HY-P4909;BDBM50526861;FA110179;CS-0674930;2-[(3S,6S,9S,12S,15R)-15-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxybutanoyl]amino]-9-benzyl-6-[(2S)-butan-2-yl]-3-(2-methylsulanylethyl)-2,5,8,11,14-pentaoxo-1-thia-4,7,10,13-tetrazacyclohexadec-12-yl]acetic acid;
Aip I, also known as Autoinducer Peptide I, is a synthetic peptide that functions as a quorum sensing molecule in Staphylococcus aureus and related bacterial species. As a member of the autoinducing peptide (AIP) family, Aip I plays a pivotal role in the regulation of the accessory gene regulator (agr) system, which orchestrates the expression of numerous virulence factors and biofilm-associated genes. Its well-defined sequence and ability to modulate intercellular communication make it a valuable tool for probing bacterial signaling pathways, understanding microbial population dynamics, and developing anti-virulence strategies in microbiological research.
Quorum sensing research: Aip I is extensively utilized in studies investigating the molecular mechanisms of quorum sensing in Gram-positive bacteria. By serving as a model autoinducing peptide, it enables researchers to dissect the agr signaling cascade, elucidate peptide-receptor interactions, and characterize the downstream regulatory networks that govern group behaviors such as toxin production and surface colonization. Its use provides crucial insights into how bacterial communities coordinate collective responses to environmental stimuli.
Biofilm formation studies: The peptide is instrumental in exploring the role of quorum sensing in biofilm development and dispersal. By modulating the concentration of Aip I in bacterial cultures, scientists can examine how agr system activation or inhibition influences biofilm architecture, maturation, and detachment. Such investigations are vital for identifying molecular targets to disrupt biofilm-associated infections and for advancing the understanding of persistent bacterial colonization on medical and industrial surfaces.
Antivirulence compound screening: Aip I serves as a reference molecule in high-throughput screening assays aimed at identifying novel inhibitors or modulators of the agr quorum sensing system. By providing a defined agonist or antagonist context, it allows for the evaluation of small molecules, peptides, or natural products that may interfere with pathogenic signaling without exerting bactericidal effects. This approach supports the development of anti-virulence strategies that minimize selective pressure for antibiotic resistance.
Peptide-receptor interaction analysis: The defined structure of Aip I makes it a preferred ligand in biochemical and biophysical studies focused on receptor binding and signal transduction. Techniques such as surface plasmon resonance, NMR spectroscopy, and fluorescence-based assays utilize the peptide to quantify binding affinities, map interaction surfaces, and investigate conformational changes upon receptor engagement. These analyses contribute to a detailed molecular understanding of peptide-mediated signaling and inform the rational design of synthetic analogs with tailored activity.
Synthetic peptide design and structure-activity relationship (SAR) studies: As a prototypical quorum sensing peptide, Aip I is frequently employed as a template for the design of structural analogs and the assessment of structure-activity relationships within the AIP family. By introducing systematic modifications to its amino acid sequence, researchers can probe the determinants of receptor specificity, agonist versus antagonist behavior, and signal potency. Such SAR studies are essential for engineering peptides with enhanced stability, selectivity, or inhibitory properties for use in advanced microbiological research and potential biotechnological applications.
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