TY  - JOUR
AU  - Almahboub, Sarah A.
AU  - Narancić, Tanja
AU  - Devocelle, Marc
AU  - Kenny, Shane T.
AU  - Palmer-Brown, William
AU  - Murphy, Cormac
AU  - Nikodinović-Runić, Jasmina
AU  - O'Connor, Kevin 
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1161
AB  - Terminal modification of peptides is frequently used to improve their hydrophobicity. While N-terminal modification with fatty acids (lipidation) has been reported previously, C-terminal lipidation is limited as it requires the use of linkers. Here we report the use of a biocatalyst for the production of an unnatural fatty amino acid, (S)-2-aminooctanoic acid (2-AOA) with enantiomeric excess  gt  98% ee and the subsequent use of 2-AOA to modify and improve the activity of an antimicrobial peptide. A transaminase originating from Chromobacterium violaceum was employed with a conversion efficiency 52-80% depending on the ratio of amino group donor to acceptor. 2-AOA is a fatty acid with amino functionality, which allowed direct C- and N-terminal conjugation respectively to an antimicrobial peptide (AMP) derived from lactoferricin B. The antibacterial activity of the modified peptides was improved by up to 16-fold. Furthermore, minimal inhibitory concentrations (MIC) of C-terminally modified peptide were always lower than N-terminally conjugated peptides. The C-terminally modified peptide exhibited MIC values of 25 mu g/ml for Escherichia coli, 50 mu g/ml for Bacillus subtilis, 100 mu g/ml for Salmonella typhimurium, 200 mu g/ml for Pseudomonas aeruginosa and 400 mu g/ml for Staphylococcus aureus. The C-terminally modified peptide was the only peptide tested that showed complete inhibition of growth of S. aureus.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Biosynthesis of 2-aminooctanoic acid and its use to terminally modify a lactoferricin B peptide derivative for improved antimicrobial activity
EP  - 799
IS  - 2
SP  - 789
VL  - 102
DO  - 10.1007/s00253-017-8655-0
ER  - 

@article{
author = "Almahboub, Sarah A. and Narancić, Tanja and Devocelle, Marc and Kenny, Shane T. and Palmer-Brown, William and Murphy, Cormac and Nikodinović-Runić, Jasmina and O'Connor, Kevin ",
year = "2018",
abstract = "Terminal modification of peptides is frequently used to improve their hydrophobicity. While N-terminal modification with fatty acids (lipidation) has been reported previously, C-terminal lipidation is limited as it requires the use of linkers. Here we report the use of a biocatalyst for the production of an unnatural fatty amino acid, (S)-2-aminooctanoic acid (2-AOA) with enantiomeric excess  gt  98% ee and the subsequent use of 2-AOA to modify and improve the activity of an antimicrobial peptide. A transaminase originating from Chromobacterium violaceum was employed with a conversion efficiency 52-80% depending on the ratio of amino group donor to acceptor. 2-AOA is a fatty acid with amino functionality, which allowed direct C- and N-terminal conjugation respectively to an antimicrobial peptide (AMP) derived from lactoferricin B. The antibacterial activity of the modified peptides was improved by up to 16-fold. Furthermore, minimal inhibitory concentrations (MIC) of C-terminally modified peptide were always lower than N-terminally conjugated peptides. The C-terminally modified peptide exhibited MIC values of 25 mu g/ml for Escherichia coli, 50 mu g/ml for Bacillus subtilis, 100 mu g/ml for Salmonella typhimurium, 200 mu g/ml for Pseudomonas aeruginosa and 400 mu g/ml for Staphylococcus aureus. The C-terminally modified peptide was the only peptide tested that showed complete inhibition of growth of S. aureus.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Biosynthesis of 2-aminooctanoic acid and its use to terminally modify a lactoferricin B peptide derivative for improved antimicrobial activity",
pages = "799-789",
number = "2",
volume = "102",
doi = "10.1007/s00253-017-8655-0"
}

Almahboub, S. A., Narancić, T., Devocelle, M., Kenny, S. T., Palmer-Brown, W., Murphy, C., Nikodinović-Runić, J.,& O'Connor, K.. (2018). Biosynthesis of 2-aminooctanoic acid and its use to terminally modify a lactoferricin B peptide derivative for improved antimicrobial activity. in Applied Microbiology and Biotechnology
Springer, New York., 102(2), 789-799.
https://doi.org/10.1007/s00253-017-8655-0

Almahboub SA, Narancić T, Devocelle M, Kenny ST, Palmer-Brown W, Murphy C, Nikodinović-Runić J, O'Connor K. Biosynthesis of 2-aminooctanoic acid and its use to terminally modify a lactoferricin B peptide derivative for improved antimicrobial activity. in Applied Microbiology and Biotechnology. 2018;102(2):789-799.
doi:10.1007/s00253-017-8655-0 .

Almahboub, Sarah A., Narancić, Tanja, Devocelle, Marc, Kenny, Shane T., Palmer-Brown, William, Murphy, Cormac, Nikodinović-Runić, Jasmina, O'Connor, Kevin , "Biosynthesis of 2-aminooctanoic acid and its use to terminally modify a lactoferricin B peptide derivative for improved antimicrobial activity" in Applied Microbiology and Biotechnology, 102, no. 2 (2018):789-799,
https://doi.org/10.1007/s00253-017-8655-0 . .