Biosynthesis of 2-aminooctanoic acid and its use to terminally modify a lactoferricin B peptide derivative for improved antimicrobial activity
Нема приказа
Аутори
Almahboub, Sarah A.Narancić, Tanja
Devocelle, Marc
Kenny, Shane T.
Palmer-Brown, William
Murphy, Cormac
Nikodinović-Runić, Jasmina
O'Connor, Kevin
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 modif...ied 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.
Кључне речи:
Unnatural amino acids / omega-Transaminase / Chromobacterium violaceum DSM30191 / Antimicrobial peptide / 2-aminooctanoic acidИзвор:
Applied Microbiology and Biotechnology, 2018, 102, 2, 789-799Издавач:
- Springer, New York
Финансирање / пројекти:
- Ministry of education of Kingdom of Saudi Arabia, King Abdullah scholarship program
DOI: 10.1007/s00253-017-8655-0
ISSN: 0175-7598
PubMed: 29177937
WoS: 000419577200025
Scopus: 2-s2.0-85034820867
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .