Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-4-16
pubmed:abstractText
Force spectroscopy between a single acetylcholinesterase (AChE) molecule and its natural substrates was performed, and the effects of inhibitors and reactivators on the force spectrum were studied with atomic force microscopy (AFM). The force spectrum between normal AChE and its substrates had its special shape. Inhibitors, which inhibit AChE by occupying the active center of the enzyme, could change the force spectrum shape noticeably. Reactivators, which reactivate the inhibited AChE by pulling the inhibitor off the active center of the enzyme, could make the normal shape of force spectrum reappear. This meant the shape features of the force spectrum could be used as a good index to observe the time course of the interactions between a single AChE molecule and its special inhibitors and reactivators in real time. The results of the real-time observation demonstrated that the inhibition times of soman and sarin on AChE were longer than 2 h and that of eserine, a reversible inhibitor of AChE, was 34 +/- 3 min. The reactivation time of HI-6 on soman-inhibited AChE was 6 +/- 2 min. These results indicated that AFM was a useful tool in pharmacology and toxicology, and could reveal time information of the interactions between AChE and its ligands.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
297
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
798-803
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Force spectroscopy between acetylcholine and single acetylcholinesterase molecules and the effects of inhibitors and reactivators studied by atomic force microscopy.
pubmed:affiliation
Institute of Pharmacology and Toxicology, Academia Sinica, Beijing, Peoples Republic of China. Zhangyg@nic.bmi.ac.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't