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Antimicrobial activity and secondary structure of a novel peptide derived from ovalbumin
Author(s) -
Tan Ao,
Suzuki Rio,
Yokoyama Chikako,
Yano Shigekazu,
Konno Hiroyuki
Publication year - 2020
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3276
Subject(s) - ovalbumin , antimicrobial , peptide , hemolysis , chemistry , hela , bacteria , antimicrobial peptides , microbiology and biotechnology , antibacterial peptide , biochemistry , antibacterial activity , biology , immunology , in vitro , immune system , genetics
A novel antimicrobial peptide derived from ovalbumin has been discovered. First, the peptide fragment RKIKVYLPRMK (TK9.1) was identified based on computerized predictions of the secondary structure of peptides in a protein data bank. Using HeliQuest, the sequence was developed into RKIKRYLRRMI (TK9.1.3), which was synthesized using Fmoc‐solid phase peptide synthesis, and found to have strongly antimicrobial activity against Gram‐positive and Gram‐negative bacteria, and fungi but not cytotoxic to HeLa cells and hemolysis in mouse red blood cells. Although ovalbumin itself does not have an antibacterial activity, our results suggest that it may supply the organisms that consume it with antimicrobial peptides, in support of their immunodefence.