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Correction: Synthesis and evaluation of nuciferine and roemerine enantiomers as 5-HT2 and α1 receptor antagonists

Hui Li Heng a, Chin Fei Chee ab, Sek Peng Chin ab, Yifan Ouyang c, Hao Wang c, Michael J. C. Buckle *a, Deron R. Herr d, Ian C. Paterson e, Stephen W. Doughty f, Noorsaadah Abd. Rahman b and Lip Yong Chung *a
aDepartment of Pharmacy, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia. E-mail: buckle@um.edu.my; chungly@um.edu.my; Fax: +60 3 79674964; Tel: +60 3 79674959
bDepartment of Chemistry, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia
cSchool of Pharmacy, Ningxia Medical University, Yinchuan, 750004, P. R. China
dDepartment of Pharmacology, Yong Loo Lin School of Medicine, National University of Singapore, 117597, Singapore
eDepartment of Oral Biology and Craniofacial Sciences and Oral Cancer Research and Coordinating Centre, Faculty of Dentistry, University of Malaya, 50603 Kuala Lumpur, Malaysia
fPenang Medical College, 4 Jalan Sepoy Lines, 10450 George Town, Pulau Pinang, Malaysia

Received 1st March 2018 , Accepted 1st March 2018

First published on 7th March 2018


Correction for ‘Synthesis and evaluation of nuciferine and roemerine enantiomers as 5-HT2 and α1 receptor antagonists’ by Hui Li Heng et al., Med. Chem. Commun., 2018, DOI: 10.1039/c7md00629b.


The authors regret that Scheme 1 showed the wrong structure for 12a, 12b, 3a and 3b. Please find below the corrected scheme.
image file: c8md90012d-s1.tif
Scheme 1

In addition, there were some errors in the numbering of two of the amino acids in Fig. 4, panels C and D. Please find below the corrected figure, including corrected caption.


image file: c8md90012d-f4.tif
Fig. 4 The docking poses of the two enantiomers of roemerine in complex with the 5-HT2A and 5-HT2C receptors. A and C. The poses of (R)-roemerine enable a π–π interaction with Phe340/328 as depicted by the black dotted lines. B and D. The poses of (S)-roemerine do not allow a π–π interaction with Phe340/328. For the purpose of clarity, only the principal binding residues are depicted and some of the transmembrane helices are not shown.

The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.


This journal is © The Royal Society of Chemistry 2018