Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents

Research output: Contribution to journal › Letter › Research › peer-review

Standard

Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents. / Craig, Alexander J.; Ermolovich, Yuri; Cameron, Alan; Rodler, Agnes; Wang, Helen; Hawkes, Jeffrey A.; Hubert, Madlen; Bjoerkling, Fredrik; Molchanova, Natalia; Brimble, Margaret A.; Moodie, Lindon W. K.; Svenson, Johan.

In: ACS Medicinal Chemistry Letters, Vol. 14, No. 6, 2023, p. 802–809.

Research output: Contribution to journal › Letter › Research › peer-review

Harvard

Craig, AJ, Ermolovich, Y, Cameron, A, Rodler, A, Wang, H, Hawkes, JA, Hubert, M, Bjoerkling, F, Molchanova, N, Brimble, MA, Moodie, LWK & Svenson, J 2023, 'Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents', ACS Medicinal Chemistry Letters, vol. 14, no. 6, pp. 802–809. https://doi.org/10.1021/acsmedchemlett.3c00093

APA

Craig, A. J., Ermolovich, Y., Cameron, A., Rodler, A., Wang, H., Hawkes, J. A., Hubert, M., Bjoerkling, F., Molchanova, N., Brimble, M. A., Moodie, L. W. K., & Svenson, J. (2023). Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents. ACS Medicinal Chemistry Letters, 14(6), 802–809. https://doi.org/10.1021/acsmedchemlett.3c00093

Vancouver

Craig AJ, Ermolovich Y, Cameron A, Rodler A, Wang H, Hawkes JA et al. Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents. ACS Medicinal Chemistry Letters. 2023;14(6):802–809. https://doi.org/10.1021/acsmedchemlett.3c00093

Author

Craig, Alexander J. ; Ermolovich, Yuri ; Cameron, Alan ; Rodler, Agnes ; Wang, Helen ; Hawkes, Jeffrey A. ; Hubert, Madlen ; Bjoerkling, Fredrik ; Molchanova, Natalia ; Brimble, Margaret A. ; Moodie, Lindon W. K. ; Svenson, Johan. / Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents. In: ACS Medicinal Chemistry Letters. 2023 ; Vol. 14, No. 6. pp. 802–809.

Bibtex

@article{b8ba7e0319c440eca9ca3fc48a4651a0,
title = "Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents",
abstract = "Small synthetic mimics of cationic antimicrobial peptides represent a promising class of compounds with leads in clinical development for the treatment of persistent microbial infections. The activity and selectivity of these compounds rely on a balance between hydrophobic and cationic components, and here, we explore the activity of 19 linear cationic tripeptides against five different pathogenic bacteria and fungi, including clinical isolates. The compounds incorporated modified hydrophobic amino acids inspired by motifs often found in bioactive marine secondary metabolites in combination with different cationic residues to probe the possibility of generating active compounds with improved safety profiles. Several of the compounds displayed high activity (low mu M concentrations), comparable with the positive controls AMC-109, amoxicillin, and amphotericin B. A higher activity was observed against the fungal strains, and a low in vitro off-target toxicity was observed against erythrocytes and HeLa cells, thereby illustrating effective means for tuning the activity and selectivity of short antimicrobial peptides.",
keywords = "Halogenated, Synthesis, Antimicrobial Peptide, Marine Natural Products, Bromotyrosine, RESISTANCE, STABILITY, MIMICS, S1",
author = "Craig, {Alexander J.} and Yuri Ermolovich and Alan Cameron and Agnes Rodler and Helen Wang and Hawkes, {Jeffrey A.} and Madlen Hubert and Fredrik Bjoerkling and Natalia Molchanova and Brimble, {Margaret A.} and Moodie, {Lindon W. K.} and Johan Svenson",
year = "2023",
doi = "10.1021/acsmedchemlett.3c00093",
language = "English",
volume = "14",
pages = "802–809",
journal = "ACS Medicinal Chemistry Letters",
issn = "1948-5875",
publisher = "American Chemical Society",
number = "6",

}

RIS

TY - JOUR

T1 - Antimicrobial Peptides Incorporating Halogenated Marine-Derived Amino Acid Substituents

AU - Craig, Alexander J.

AU - Ermolovich, Yuri

AU - Cameron, Alan

AU - Rodler, Agnes

AU - Wang, Helen

AU - Hawkes, Jeffrey A.

AU - Hubert, Madlen

AU - Bjoerkling, Fredrik

AU - Molchanova, Natalia

AU - Brimble, Margaret A.

AU - Moodie, Lindon W. K.

AU - Svenson, Johan

PY - 2023

Y1 - 2023

N2 - Small synthetic mimics of cationic antimicrobial peptides represent a promising class of compounds with leads in clinical development for the treatment of persistent microbial infections. The activity and selectivity of these compounds rely on a balance between hydrophobic and cationic components, and here, we explore the activity of 19 linear cationic tripeptides against five different pathogenic bacteria and fungi, including clinical isolates. The compounds incorporated modified hydrophobic amino acids inspired by motifs often found in bioactive marine secondary metabolites in combination with different cationic residues to probe the possibility of generating active compounds with improved safety profiles. Several of the compounds displayed high activity (low mu M concentrations), comparable with the positive controls AMC-109, amoxicillin, and amphotericin B. A higher activity was observed against the fungal strains, and a low in vitro off-target toxicity was observed against erythrocytes and HeLa cells, thereby illustrating effective means for tuning the activity and selectivity of short antimicrobial peptides.

AB - Small synthetic mimics of cationic antimicrobial peptides represent a promising class of compounds with leads in clinical development for the treatment of persistent microbial infections. The activity and selectivity of these compounds rely on a balance between hydrophobic and cationic components, and here, we explore the activity of 19 linear cationic tripeptides against five different pathogenic bacteria and fungi, including clinical isolates. The compounds incorporated modified hydrophobic amino acids inspired by motifs often found in bioactive marine secondary metabolites in combination with different cationic residues to probe the possibility of generating active compounds with improved safety profiles. Several of the compounds displayed high activity (low mu M concentrations), comparable with the positive controls AMC-109, amoxicillin, and amphotericin B. A higher activity was observed against the fungal strains, and a low in vitro off-target toxicity was observed against erythrocytes and HeLa cells, thereby illustrating effective means for tuning the activity and selectivity of short antimicrobial peptides.

KW - Halogenated

KW - Synthesis

KW - Antimicrobial Peptide

KW - Marine Natural Products

KW - Bromotyrosine

KW - RESISTANCE

KW - STABILITY

KW - MIMICS

KW - S1

U2 - 10.1021/acsmedchemlett.3c00093

DO - 10.1021/acsmedchemlett.3c00093

M3 - Letter

C2 - 37312845

VL - 14

SP - 802

EP - 809

JO - ACS Medicinal Chemistry Letters

JF - ACS Medicinal Chemistry Letters

SN - 1948-5875

IS - 6

ER -

ID: 348205370