Magnetic microsphere-based methods to study the interaction of teicoplanin with peptides and bacteria.

Analytical and Bioanalytical Chemistry
Menake E PiyasenaFrank A Gomez

Abstract

Teicoplanin (teic) from Actinoplanes teichomyceticus is a glycopeptide antibiotic used to treat many gram-positive bacterial infections. Glycopeptide antibiotics inhibit bacterial growth by binding to carboxy-terminal D-Ala-D-Ala intermediates in the peptidoglycan of the cell wall of gram-positive bacteria. In this paper we report the derivatization of magnetic microspheres with teic (teic-microspheres). Fluorescence-based techniques have been developed to analyze the binding properties of the microspheres to two D-Ala-D-Ala terminus peptides. The dissociation constant for the binding of carboxyfluorescein-labeled D-Ala-D-Ala-D-Ala to teic on microspheres was established via fluorimetry and flow cytometry and was determined to be 0.5 x 10(-6) and 3.0 x 10(-6) mol L(-1), respectively. The feasibility of utilizing microparticles with fluorescence methods to detect low levels (the limit of bacterial detection was determined to be 30 colon-forming units; cfu) of gram-positive bacteria has been demonstrated. A simple microfluidic experiment is reported to demonstrate the possibility of developing microsphere-based affinity assays to study peptide-antibiotic interaction.

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Citations

Jul 1, 2009·Bioanalysis·Maral SarakhanikhoramiFrank A Gomez
Jun 18, 2011·Expert Review of Proteomics·Mingxia GaoXiangmin Zhang
Aug 4, 2010·Analytica Chimica Acta·K Aguilar-ArteagaE Barrado
Dec 9, 2010·Langmuir : the ACS Journal of Surfaces and Colloids·Lev BrombergCarmen Alvarez-Lorenzo

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Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

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