TY - JOUR
T1 - Fluorescent labeling of nisin Z and assessment of anti-listerial action
AU - Imran, Muhammad
AU - Revol-Junelles, A.-M.
AU - Diepeveen-de Bruin, M.
AU - Paris, C.
AU - Breukink, E.J.
AU - Desobry, S.
PY - 2013
Y1 - 2013
N2 - Biomolecule labeling by fluorescent markers has emerged as an innovative methodology for bio-analytical purposes
in foodmicrobiology, medicine and pharmaceutics due to the great advantages of thismethod such as precision,
wide detection limits, and in vivo recognition. Fluorescent nisin Z was synthesized by linking the carboxyl
group and amino group of nisin Z and 5-aminoacetamido fluorescein (AAA-flu). This new structure was fully
characterized by mass spectrometry with a molecular weight of 3717.3 Da. Intracellular K+ leakage and transmembrane
electrical potential (Δψ)were used to evaluate the antibacterial action of the labeledmolecule against
three listerial strains and demonstrated that nisin Z endured the labeling processwithout any activity loss. In vivo
activity of labeled nisin was observed by confocal laser microscope which revealed its localization at the septum
of listerial cell division sitewhere themembrane-bound cellwall precursor lipid II ismaximal. Fluorescent nisin Z
showed its great potential as a tool to study antibacterial mechanism of action of nisin in biological systems
AB - Biomolecule labeling by fluorescent markers has emerged as an innovative methodology for bio-analytical purposes
in foodmicrobiology, medicine and pharmaceutics due to the great advantages of thismethod such as precision,
wide detection limits, and in vivo recognition. Fluorescent nisin Z was synthesized by linking the carboxyl
group and amino group of nisin Z and 5-aminoacetamido fluorescein (AAA-flu). This new structure was fully
characterized by mass spectrometry with a molecular weight of 3717.3 Da. Intracellular K+ leakage and transmembrane
electrical potential (Δψ)were used to evaluate the antibacterial action of the labeledmolecule against
three listerial strains and demonstrated that nisin Z endured the labeling processwithout any activity loss. In vivo
activity of labeled nisin was observed by confocal laser microscope which revealed its localization at the septum
of listerial cell division sitewhere themembrane-bound cellwall precursor lipid II ismaximal. Fluorescent nisin Z
showed its great potential as a tool to study antibacterial mechanism of action of nisin in biological systems
U2 - 10.1016/j.mimet.2013.07.009
DO - 10.1016/j.mimet.2013.07.009
M3 - Article
SN - 0167-7012
VL - 95
SP - 107
EP - 113
JO - Journal of Microbiological Methods
JF - Journal of Microbiological Methods
IS - 2
ER -