Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma. / Hein-Kristensen, Line; Knapp, Kolja M; Franzyk, Henrik; Gram, Lone.

In: Research in Microbiology, Vol. 164, No. 9, 27.08.2013, p. 933-940.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hein-Kristensen, L, Knapp, KM, Franzyk, H & Gram, L 2013, 'Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma', Research in Microbiology, vol. 164, no. 9, pp. 933-940. https://doi.org/10.1016/j.resmic.2013.08.002

APA

Hein-Kristensen, L., Knapp, K. M., Franzyk, H., & Gram, L. (2013). Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma. Research in Microbiology, 164(9), 933-940. https://doi.org/10.1016/j.resmic.2013.08.002

Vancouver

Hein-Kristensen L, Knapp KM, Franzyk H, Gram L. Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma. Research in Microbiology. 2013 Aug 27;164(9):933-940. https://doi.org/10.1016/j.resmic.2013.08.002

Author

Hein-Kristensen, Line ; Knapp, Kolja M ; Franzyk, Henrik ; Gram, Lone. / Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma. In: Research in Microbiology. 2013 ; Vol. 164, No. 9. pp. 933-940.

Bibtex

@article{6f649d743fae4cef8e3ea4b397c2af80,
title = "Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma",
abstract = "Antimicrobial peptides (AMPs) are promising leads for novel antibiotics; however, their activity is often compromised under physiological conditions. The purpose of this study was to determine the activity of α-peptide/β-peptoid peptidomimetics and AMPs against Escherichia coli and Staphylococcus aureus in the presence of human blood-derived matrices and immune effectors. The minimum inhibitory concentration (MIC) of two peptidomimetics against E. coli decreased by up to one order of magnitude when determined in 50% blood plasma as compared to MHB media. The MIC of a membrane-active AMP, LL-I/3 also decreased, whereas two intracellularly acting AMPs were not potentiated by plasma. Blood serum had no effect on activity against E. coli and neither matrix had an effect on activity against S. aureus. Unexpectedly, physiological concentrations of human serum albumin did not influence activity. Plasma potentiation was not caused by an LL-37 analogue, lysozyme or hydrogen peroxide; however, plasma potentiation of activity was abolished when the complement system was heat-inactivated. Time-course experiments indicated that potentiation was due to plasma-mediated effects on bacterial cells prior to activities of peptidomimetics. The unexpected enhancement of antibacterial activity of peptidomimetics and AMPs under physiological conditions significantly increases the therapeutic potential of these compounds.",
author = "Line Hein-Kristensen and Knapp, {Kolja M} and Henrik Franzyk and Lone Gram",
note = "Copyright {\textcopyright} 2013. Published by Elsevier Masson SAS.",
year = "2013",
month = aug,
day = "27",
doi = "10.1016/j.resmic.2013.08.002",
language = "English",
volume = "164",
pages = "933--940",
journal = "Research in Microbiology",
issn = "0923-2508",
publisher = "Elsevier Masson",
number = "9",

}

RIS

TY - JOUR

T1 - Selectivity in the potentiation of antibacterial activity of α-peptide/β-peptoid peptidomimetics and antimicrobial peptides by human blood plasma

AU - Hein-Kristensen, Line

AU - Knapp, Kolja M

AU - Franzyk, Henrik

AU - Gram, Lone

N1 - Copyright © 2013. Published by Elsevier Masson SAS.

PY - 2013/8/27

Y1 - 2013/8/27

N2 - Antimicrobial peptides (AMPs) are promising leads for novel antibiotics; however, their activity is often compromised under physiological conditions. The purpose of this study was to determine the activity of α-peptide/β-peptoid peptidomimetics and AMPs against Escherichia coli and Staphylococcus aureus in the presence of human blood-derived matrices and immune effectors. The minimum inhibitory concentration (MIC) of two peptidomimetics against E. coli decreased by up to one order of magnitude when determined in 50% blood plasma as compared to MHB media. The MIC of a membrane-active AMP, LL-I/3 also decreased, whereas two intracellularly acting AMPs were not potentiated by plasma. Blood serum had no effect on activity against E. coli and neither matrix had an effect on activity against S. aureus. Unexpectedly, physiological concentrations of human serum albumin did not influence activity. Plasma potentiation was not caused by an LL-37 analogue, lysozyme or hydrogen peroxide; however, plasma potentiation of activity was abolished when the complement system was heat-inactivated. Time-course experiments indicated that potentiation was due to plasma-mediated effects on bacterial cells prior to activities of peptidomimetics. The unexpected enhancement of antibacterial activity of peptidomimetics and AMPs under physiological conditions significantly increases the therapeutic potential of these compounds.

AB - Antimicrobial peptides (AMPs) are promising leads for novel antibiotics; however, their activity is often compromised under physiological conditions. The purpose of this study was to determine the activity of α-peptide/β-peptoid peptidomimetics and AMPs against Escherichia coli and Staphylococcus aureus in the presence of human blood-derived matrices and immune effectors. The minimum inhibitory concentration (MIC) of two peptidomimetics against E. coli decreased by up to one order of magnitude when determined in 50% blood plasma as compared to MHB media. The MIC of a membrane-active AMP, LL-I/3 also decreased, whereas two intracellularly acting AMPs were not potentiated by plasma. Blood serum had no effect on activity against E. coli and neither matrix had an effect on activity against S. aureus. Unexpectedly, physiological concentrations of human serum albumin did not influence activity. Plasma potentiation was not caused by an LL-37 analogue, lysozyme or hydrogen peroxide; however, plasma potentiation of activity was abolished when the complement system was heat-inactivated. Time-course experiments indicated that potentiation was due to plasma-mediated effects on bacterial cells prior to activities of peptidomimetics. The unexpected enhancement of antibacterial activity of peptidomimetics and AMPs under physiological conditions significantly increases the therapeutic potential of these compounds.

U2 - 10.1016/j.resmic.2013.08.002

DO - 10.1016/j.resmic.2013.08.002

M3 - Journal article

C2 - 23994143

VL - 164

SP - 933

EP - 940

JO - Research in Microbiology

JF - Research in Microbiology

SN - 0923-2508

IS - 9

ER -

ID: 50759911