PR 39 (porcine) is a proline-rich antimicrobial peptide known for flexible, extended conformations and strong protein-binding capability. The sequence facilitates exploration of proteasome engagement, membrane interaction, and structural plasticity. Researchers use it to probe charge-mediated folding and hydrophobic clustering. Its unique composition supports advanced biophysical characterization.
CAT No: R0893
CAS No:139637-11-9
Synonyms/Alias:139637-11-9;PR 39;PR-39;CHEBI:131850;DTXSID90161139;CID 16198954;RRRPRPPYLPRPRPPPFFPPRLPPRIPPGFPPRFPPRFP;H-Arg-Arg-Arg-Pro-Arg-Pro-Pro-Tyr-Leu-Pro-Arg-Pro-Arg-Pro-Pro-Pro-Phe-Phe-Pro-Pro-Arg-Leu-Pro-Pro-Arg-Ile-Pro-Pro-Gly-Phe-Pro-Pro-Arg-Phe-Pro-Pro-Arg-Phe-Pro-OH;H-L-Arg-L-Arg-L-Arg-L-Pro-L-Arg-L-Pro-L-Pro-L-Tyr-L-Leu-L-Pro-L-Arg-L-Pro-L-Arg-L-Pro-L-Pro-L-Pro-L-Phe-L-Phe-L-Pro-L-Pro-L-Arg-L-Leu-L-Pro-L-Pro-L-Arg-L-Ile-L-Pro-L-Pro-Gly-L-Phe-L-Pro-L-Pro-L-Arg-L-Phe-L-Pro-L-Pro-L-Arg-L-Phe-L-Pro-NH2;L-Arg-L-Arg-L-Arg-L-Pro-L-Arg-L-Pro-L-Pro-L-Tyr-L-Leu-L-Pro-L-Arg-L-Pro-L-Arg-L-Pro-L-Pro-L-Pro-L-Phe-L-Phe-L-Pro-L-Pro-L-Arg-L-Leu-L-Pro-L-Pro-L-Arg-L-Ile-L-Pro-L-Pro-Gly-L-Phe-L-Pro-L-Pro-L-Arg-L-Phe-L-Pro-L-Pro-L-Arg-L-Phe-L-Pro;DTXCID4083630;DA-61996;
PR 39 (porcine) is a naturally occurring antimicrobial peptide originally identified in pig leukocytes, notable for its proline- and arginine-rich sequence and potent biological activities. As a member of the cathelicidin family, it plays a significant role in innate immune defense by disrupting microbial membranes and modulating inflammatory responses. Its unique structure and multifunctional properties have made it an important tool in peptide research, particularly in the fields of host-pathogen interactions, immunology, and cell signaling. The peptide's ability to interact with various biological targets has prompted extensive investigation into its mechanisms of action and potential utility in experimental systems.
Antimicrobial mechanism studies: PR 39 is widely utilized to elucidate the molecular basis of antimicrobial activity in innate immune systems. Its ability to permeabilize bacterial membranes and interfere with essential cellular processes makes it a valuable model for studying peptide-microbe interactions. Researchers employ this peptide in assays designed to characterize the kinetics and specificity of antimicrobial action, enabling a deeper understanding of how host defense peptides contribute to pathogen clearance and resistance mechanisms.
Innate immunity and inflammation research: The peptide's immunomodulatory properties are of significant interest in studies exploring the regulation of inflammatory responses. Investigations often use PR 39 to examine its influence on cytokine production, leukocyte chemotaxis, and the modulation of inflammatory signaling cascades. These studies provide insight into the dual antimicrobial and immunoregulatory functions of cathelicidins, supporting broader efforts to map the interplay between host defense peptides and immune cell behavior.
Peptide structure-activity relationship analysis: PR 39 serves as a model substrate for structure-activity relationship (SAR) studies, where its sequence is systematically modified to assess the impact of specific amino acid residues on biological function. Such research advances the understanding of how peptide conformation, charge distribution, and hydrophobicity dictate interaction with microbial membranes and host receptors. SAR investigations using this peptide inform the rational design of novel peptides with tailored functional profiles for research applications.
Cell signaling and gene regulation investigations: Due to its reported influence on intracellular signaling pathways and gene expression, PR 39 is employed in experiments probing the modulation of cellular processes such as apoptosis, proliferation, and differentiation. Researchers leverage its capacity to interact with signaling molecules and transcriptional regulators to dissect the downstream effects of peptide-mediated signaling in various cell types, particularly within the context of immune and epithelial cells.
Peptide delivery and stability studies: The stability and functional retention of PR 39 in diverse biological environments make it a suitable candidate for testing peptide delivery systems and assessing proteolytic resistance. Scientists use the peptide to evaluate encapsulation methods, carrier systems, and formulation approaches designed to enhance peptide bioavailability and durability in vitro. These applications contribute to the broader field of peptide engineering, informing strategies for the effective delivery and stabilization of bioactive peptides in research settings.
PR-39 peptide was first isolated from the small intestine of a pig exhibiting antibacterial activity against both Escherichia coli and Bacillus megaterium. Four years after its discovery i.e. in 1995, the PR-39 gene was sequenced. Recent research has indicated that PR-39 is a multi-functional peptide and a mainstay of the innate immune system. There is increasing evidence that PR-39 promotes angiogenesis, wound healing, leukocyte chemotaxis and inhibits bacterial DNA and protein synthesis.
Proline-arginine rich (PR-39) cathelicidin: Structure, expression and functional implication in intestinal health
Recently, PR-39 was found in wound fluid and was shown to have inductive activity on matrix components as part of the wound repair process. We have now sequenced the complete gene and possible mediators of its expression will be discussed. Our attempts to characterize the human counterpart of PR-39 by probing for the well conserved prepro-part led to a different peptide antibiotic.
PR-39, a proline-rich peptide antibiotic from pig, and FALL-39, a tentative human counterpart
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