Literature DB >> 15453475

Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose peptone.

S Campagna1, A-G Mathot, Y Fleury, J M Girardet, J L Gaillard.   

Abstract

A synthetic peptide of 23 residues corresponding to the carboxyterminal 113 to 135 region of component-3 of proteose peptone (PP3) has been investigated with regard to its antibacterial properties. This cationic amphipathic peptide that we refer to as lactophoricin, displayed a growth-inhibitory activity against both gram-positive and gram-negative bacteria. For most of the strains tested, bacterial growth was observed in the presence of lactophoricin except for Streptococcus thermophilus. In that case, lactophoricin exhibited a minimum inhibitory concentration of 10 microM and a minimum lethal concentration of 20 microM. No hemolysis of human red blood cells was detected for peptide concentrations between 2 to 200 microM, indicating that lactophoricin would be noncytotoxic when used in this concentration range.

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Year:  2004        PMID: 15453475     DOI: 10.3168/jds.S0022-0302(04)73316-0

Source DB:  PubMed          Journal:  J Dairy Sci        ISSN: 0022-0302            Impact factor:   4.034


  9 in total

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7.  Structural and Mechanismic Studies of Lactophoricin Analog, Novel Antibacterial Peptide.

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Journal:  Int J Mol Sci       Date:  2021-04-02       Impact factor: 5.923

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  9 in total

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