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Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes
Author(s) -
Harwig Sylvia S.L,
Kokryakov Vladimir N,
Swiderek Kristine M,
Aleshina Galina M,
Zhao Chengquan,
Lehrer Robert I
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00210-z
Subject(s) - peptide , listeria monocytogenes , antimicrobial , proline , in vitro , bacteria , antimicrobial peptides , biochemistry , chemistry , biology , microbiology and biotechnology , amino acid , genetics
We purified and characterized an unusual antimicrobial peptide, prophenin‐1 (PF‐1), from porcine leukocytes. The peptide had a mass of 8,683 and contained 79 residues, including 42 (53.2%) prolines and 15 (19.0%) phenylalanines. Its N‐terminal 60 residues consisted of three perfect and three nearly perfect repeats of a decamer, FPPPNFPGPR. Prophenin‐1 was encoded on a cathelin‐containing precursor and showed substantially more activity against E. coli , a Gram‐negative bacterium, than against Listeria monocytogenes , a Gram‐positive organism, in vitro.