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Chang, T.W.* ; Blank, M. ; Janardhanan, P.* ; Singh, B.R.* ; Mello, C.* ; Blind, M.* ; Cai, S.W.*

In vitro selection of RNA aptamers that inhibit the activity of type A botulinum neurotoxin.

Biochem. Biophys. Res. Commun. 396, 854-860 (2010)
DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The category A agent, botulinum neurotoxin (BoNT), is the most toxic molecule known to mankind. The endopeptidase activity of light chain domain of BoNT is the cause for the inhibition of the neurotransmitter release and the flaccid paralysis that leads to lethality in botulism. Currently, antidotes are not available to reverse the flaccid paralysis caused by BoNT. In the present study, we have identified three RNA aptamers through SELEX-process, which bind strongly to the light chain of type A BoNT (BoNT/A) and inhibit the endopeptidase activity, with IC50 in low nM range. Inhibition kinetic studies reveal low nM K-1 and non-competitive nature of their inhibition. Aptamers are unique group of molecules as therapeutics, and this is first report of their development as an antidote against botulism. These data on K-1 and IC50 strongly suggest that the aptamers have strong potential as antidotes that can reverse the symptom caused by BoNT/A.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter RNA; Aptamer; Botulinum neurotoxin; Antidote; Endopeptidase
Sprache englisch
Veröffentlichungsjahr 2010
HGF-Berichtsjahr 2010
ISSN (print) / ISBN 0006-291X
e-ISSN 1090-2104
Zeitschrift Biochemical and Biophysical Research Communications
Quellenangaben Band: 396, Heft: 4, Seiten: 854-860 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort San Diego
Begutachtungsstatus Peer reviewed
Institut(e) CCG Hematopoetic Cell Transplants (IMI-KHZ)
POF Topic(s) 30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Forschungsfeld(er) Immune Response and Infection
PSP-Element(e) G-520300-001
DOI 10.1016/j.bbrc.2010.05.006
Scopus ID 77953289484
Erfassungsdatum 2010-12-31
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