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 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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