Synthesis, antimicrobial activity, attenuation of aminoglycoside resistance in MRSA, and ribosomal A-site binding of pyrene-neomycin conjugates.


Journal

European journal of medicinal chemistry
ISSN: 1768-3254
Titre abrégé: Eur J Med Chem
Pays: France
ID NLM: 0420510

Informations de publication

Date de publication:
01 Feb 2019
Historique:
received: 26 07 2018
revised: 07 11 2018
accepted: 08 11 2018
pubmed: 12 12 2018
medline: 12 2 2019
entrez: 12 12 2018
Statut: ppublish

Résumé

The development of new ligands that have comparable or enhanced therapeutic efficacy relative to current drugs is vital to the health of the global community in the short and long term. One strategy to accomplish this goal is to functionalize sites on current antimicrobials to enhance specificity and affinity while abating resistance mechanisms of infectious organisms. Herein, we report the synthesis of a series of pyrene-neomycin B (PYR-NEO) conjugates, their binding affinity to A-site RNA targets, resistance to aminoglycoside-modifying enzymes (AMEs), and antibacterial activity against a wide variety of bacterial strains of clinical relevance. PYR-NEO conjugation significantly alters the affinities of NEO for bacterial A-site targets. The conjugation of PYR to NEO significantly increased the resistance of NEO to AME modification. PYR-NEO conjugates exhibited broad-spectrum activity towards Gram-positive bacteria, including improved activity against NEO-resistant methicillin-resistant Staphylococcus aureus (MRSA) strains.

Identifiants

pubmed: 30530174
pii: S0223-5234(18)30980-2
doi: 10.1016/j.ejmech.2018.11.022
pmc: PMC6503653
mid: NIHMS1516202
pii:
doi:

Substances chimiques

Aminoglycosides 0
Pyrenes 0
Ribosomal Proteins 0
Framycetin 4BOC774388
ribosomal protein L7-L12 70815-33-7

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

381-393

Subventions

Organisme : NIAID NIH HHS
ID : R41 AI126874
Pays : United States
Organisme : NIGMS NIH HHS
ID : R42 GM097917
Pays : United States
Organisme : NIGMS NIH HHS
ID : R41 GM097917
Pays : United States
Organisme : NIDCD NIH HHS
ID : R41 DC016257
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI090048
Pays : United States

Informations de copyright

Copyright © 2018 Elsevier Masson SAS. All rights reserved.

Auteurs

Sandra Story (S)

NUBAD, LLC, Greenville, SC, 29605, United States.

Michael J Skriba (MJ)

Department of Chemistry, Clemson University, Clemson, SC, 29634, United States.

Krishnagopal Maiti (K)

Department of Chemistry, Clemson University, Clemson, SC, 29634, United States.
Department of Medicinal Chemistry, National Institute of Pharmaceutical Education and Research (NIPER), Raebareli, 229010, India.

Natalya N Degtyareva (NN)

NUBAD, LLC, Greenville, SC, 29605, United States.

Keith D Green (KD)

College of Pharmacy, University of Kentucky, Lexington, KY, 40536-0596, United States.

Verjine Khodaverdian (V)

School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332-0400, United States.

Adegboyega K Oyelere (AK)

School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332-0400, United States; Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, 30332, United States.

Sylvie Garneau-Tsodikova (S)

College of Pharmacy, University of Kentucky, Lexington, KY, 40536-0596, United States.

Dev P Arya (DP)

NUBAD, LLC, Greenville, SC, 29605, United States; Department of Chemistry, Clemson University, Clemson, SC, 29634, United States. Electronic address: dparya@clemson.edu.

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Classifications MeSH