Preparation of secolycorines against acetylcholinesterase

Lee, Shoei‐Sheng; Venkatesham, U.; Rao, Chitneni Prasad; Lam, Sio Hong; Lin, Jiunn-Yuan

doi:10.1016/j.bmc.2006.10.026

Cited by 38 publications

(31 citation statements)

References 16 publications

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“…These values fell within the reported electric eel AChE IC 50 inhibition data for galantamine (0.55 lM [21]; 3.18 lM [22]), and tacrine (0.044 lM [23]; 0.18 lM [24]). The AChE inhibition assays, monitored by HPLC, showed that sulfenamides were stable throughout the experiment, suggesting that they are responsible for the inhibition, and ruled out the possibility of any inhibitory activity due to their hydrolysis products.…”

Section: Resultssupporting

confidence: 65%

Novel sulfenamides as promising acetylcholinesterase inhibitors

Proença

Serralheiro

Araújo

et al. 2011

Journal of Heterocyclic Chem

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Several sulfenamide derivatives were designed as possible acetylcholinesterase (AChE) inhibitors. New sulfenamides were synthesized and proved to be stable under the physiological conditions used in the enzymatic assays. N‐benzyl‐2‐benzoxazolylsulfenamide (8) and N‐benzyl‐2‐benzimidazolylsulfenamide (9) revealed anti‐AChE activity with IC50 values of 0.6 and 0.8 μM, respectively, values of the same magnitude as those reported for galantamine and tacrine. The affinity for the biological site was evaluated in terms of interaction/partition toward sodium dodecyl sulfate (SDS) micelles. The inhibitory activity profiles were reasoned in terms of both partition toward a hydrophobic anionic environment and molecular geometry. The XCSN dihedral angle deviations from collinearity stood out as a major parameter linked to enzyme specificity. J. Heterocyclic Chem., (2011).

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Section: Resultssupporting

confidence: 65%

Novel sulfenamides as promising acetylcholinesterase inhibitors

Proença

Serralheiro

Araújo

et al. 2011

Journal of Heterocyclic Chem

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“…Afford compound 21-26, compound obtained by in vitro tests found that the open-loop E ring did not affect its activity, but may be due to the changes of solubility and increased its activity. The results of this study indicate that the aromaticity of D rings enhances the inhibitory activity of anti-AChE activity [11] . …”

Section: Modification Of a Ringmentioning

confidence: 62%

Review on the Structure Modification of Lycorine

Yu-bin

Yang

Zhang

et al. 2017

IOP Conf. Ser.: Earth Environ. Sci.

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“…Apart from this, the ring C aromatized lycorine variant assoanine 9 has been described as a potent inhibitor with IC 50 at 3.87 M while activity for its 6-oxo analog (oxoassoanine 10) was moderated to 47.21 M (Lopez et al, 2002). Furthermore, the 2-hydroxy substituted, ring C aromatized lycorine variant ungerimine 11 is reportedly a moderate inhibitor (IC 50 86 M) (Houghton et al, 2006), while several semi-synthetic ring D seco-lycorine analogs possessing a planar dihydrophenanthridine nucleus are reputedly highly efficient at AChE inhibition with the most potent of these effective at 2.66 M (Lee et al, 2007) (Fig. 1).…”

Section: Resultsmentioning

confidence: 94%