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pro vyhledávání: '"Ji-Sun Kim"'
Publikováno v:
Journal of Microbiology and Biotechnology. 28:1299-1309
We previously reported on lactophoricin (LPcin), a cationic α-helical antimicrobial peptide derived from bovine milk, which has antimicrobial effects on Candida albicans as well as Gram-positive and Gram-negative bacteria. In this study, we designed
Publikováno v:
Journal of microbiology and biotechnology. 28(3)
We have previously derived a novel antimicrobial peptide, LPcin-YK3(YK3), based on lactophoricin and have successfully studied and reported on the relationship between its structure and function. In this study, antimicrobial peptides with improved an
Publikováno v:
Journal of microbiology and biotechnology. 27(4)
Lactophoricin (LPcin), which is a part of proteose peptone isolated from bovine milk, is a cationic amphipathic α-helical antimicrobial peptide. Its truncated variants and mutated analogs were designed and their antimicrobial activities were evaluat
Publikováno v:
Protein Expression and Purification. 65:23-29
Lactophoricin (LPcin-I) is a 23-amino acid peptide that corresponds to the carboxyterminal 113–135 region of component-3 of proteose peptone (PP3), a minor phosphoglycoprotein found in bovine milk. It has been reported that lactophoricin has antiba
Publikováno v:
Biophysical journal. 101(5)
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not