Concise Article
MedChemComm
encoded potassium channel (e.g. 26; IC50 > 30 mM), or the cyto- 3 D. Matsuda and H. Tomoda, Curr. Opin. Invest. Drugs, 2007,
chrome P450 enzyme isoforms CYP1A2, CYP2C9, CYP2C19,
CYP2D6 and CYP3A4 (e.g. 26; all IC50s > 10 mM). Compounds in
this series were also tested to conrm in vivo inhibition of DGAT-1
8, 836.
4 H. C. Chen and R. V. Farese, Arterioscler., Thromb., Vasc. Biol.,
2005, 25, 482.
using a rat oral lipid tolerance test.5 Treatment with 26 resulted in 5 A. M. Birch, S. Birtles, L. K. Buckett, P. D. Kemmitt,
an exposure-dependent decrease in circulating plasma triglyc-
eride levels. Fig. 4 shows the relationship between plasma
G. J. Smith, T. J. D. Smith, A. V. Turnbull and
S. J. Y. Wang, J. Med. Chem., 2009, 52, 1558.
triglycerides and free compound levels in plasma for 26 in this 6 W. McCoull, M. S. Addie, A. M. Birch, S. Birtles, L. K. Buckett,
model. PK-PD analysis indicates that the in vivo generated free
IC50 (0.2 nM) is in good agreement with the in vitro IC50 in rat
microsomes (0.9 nM) and a functional cell assay measuring
triglyceride synthesis in the HuTu80 human cell line (4 nM).
R. J. Butlin, S. S. Bowker, S. Boyd, S. Chapman,
R. D. M. Davies, C. S. Donald, C. P. Green, C. Jenner,
P. D. Kemmitt, A. G. Leach, G. C. Moody, P. Morentin
Gutierrez, N. J. Newcombe, T. Nowak, M. J. Packer,
A. T. Plowright, J. Revill, P. Schoeld, C. Sheldon, S. Stokes,
A. V. Turnbull, S. J. Y. Wang, D. P. Whalley and
J. M. Wood, Bioorg. Med. Chem. Lett., 2012, 22, 3873.
7 M. J. Waring, A. M. Birch, S. Birtles, L. K. Buckett, R. J. Butlin,
L. Campbell, P. Morentin Gutierrez, P. D. Kemmitt,
A. G. Leach, P. A. MacFaul, C. O’Donnell and
A. V. Turnbull, Med. Chem. Commun., submitted for
publication.
Conclusion
In summary, a novel series of hDGAT-1 inhibitors is described.
Design hypotheses were devised to introduce changes in shape
and polarity into the side chain, reduce lipophilicity and mask
the hydrogen bond donors with internal hydrogen bond
acceptors to improve the solubility and unbound clearance
prole of the clinical candidate 1. These changes led to the 8 R. L. Dow, J. Li, M. P. Pence, E. M. Gibbs, J. L. LaPerle,
replacement of the phenyl cyclohexyl-ethanoate side chain, a
fragment present in a number of hDGAT-1 inhibitors, with
substituted oxy-linked side chains. Combining the best features
of two sub-series, including balancing lipophilicity and
permeability, provided potent inhibitors of hDGAT-1 and dis-
played increased solubility and excellent ADMET parameters,
whilst maintaining good properties such as LLE. Simulta-
neously, greater selectivity against the related enzyme hACAT-1
J. Litcheld, D. W. Piotrowski, M. J. Munchhof,
T. B. Manion, W. J. Zavadoski, G. S. Walker,
R. K. McPherson, S. Tapley, E. Sugarman, A. Guzman-Perez
and P. DaSilva-Jardine, ACS Med. Chem. Lett., 2011, 2, 407.
9 R. L. Dow, M. Andrews, G. E. Aspnes, G. Balan, E. M. Gibbs,
A. Guzman-Perez, K. Karki, J. L. LaPerle, J. Li, J. Litcheld,
M. J. Munchhof, C. Perreault and L. Patel, Bioorg. Med.
Chem. Lett., 2011, 21, 6122.
was achieved. The comparison of the small molecule X-ray 10 V. S. C. Yeh, D. W. A. Beno, S. Brodjian, M. E. Brune,
structures of 4 and 28 shows marked differences in the solid
state. Compound 28 adopts a different shape due to the axial
positioning of the cis-oxy-pyridyl group. The planes of the
molecules are held together by van der Waals interactions,
including p–p stacking, and each molecule is involved in a
dimeric pairing leading to an overall decreased packing effi-
ciency of 28. Finally, inhibition of DGAT-1 in vitro translates to
S. C. Cullen, B. D. Dayton, M. K. Dhaon, H. D. Falls,
J. Gao, N. Grihalde, P. Hajduk, T. M. Hansen, A. S. Judd,
A. J. King, R. C. Klix, K. J. Larson, Y. Y. Lau, K. C. Marsh,
S. W. Mittelstadt, D. Plata, M. J. Rozema, J. A. Segreti,
E. J. Stoner, M. J. Voorbach, X. Wang, X. Xin, G. Zhao,
C. A. Collins, B. F. Cox, R. M. Reilly, P. R. Kym and
A. J. Souers, J. Med. Chem., 2012, 55, 1751.
lating plasma triglyceride levels in an exposure-dependent
manner in a rat oral lipid tolerance test.
908&rank¼1.
12 log D, plasma-protein binding and solubility measurements
were made as described in: D. Buttar, N. Colclough,
S. Gerhardt, P. A. MacFaul, S. D. Phillips, A. T. Plowright,
P. Whittamore, K. Tam, K. Maskos, S. Steinbacher and
H. Steuber, Bioorg. Med. Chem., 2010, 18, 7486.
Acknowledgements
The research was sponsored by AstraZeneca. All authors were
employees of AstraZeneca at the time of the research. The authors 13 S. Cases, S. J. Smith, Y. W. Zheng, H. M. Myers, T.-Y. Chang,
thank Scott Boyd, Craig Donald, Kristin Goldberg and Adele Lloyd
for the synthesis and purication of test compounds, Usha
B.-L. Li, C. C. Y. Chang, Y. Urano and Y. Am., J. Endocrinol.
Metab., 2009, 297, E1–E9.
Chauhan for the testing of compounds in biological assays and 14 E. Floetmann, L. K. Buckett, A. V. Turnbull, C. Hammond,
colleagues in Physical Chemistry, DMPK and safety assessment
for the provision of secondary ADMET data.
C. Hallberg, A. Birch, D. Lees and H. B. Jones, manuscript
in preparation.
15 M. J. Waring, Bioorg. Med. Chem. Lett., 2009, 19, 2844.
16 X-ray data for compound 4: molecular formula
¼
Notes and references
C
23H21F3N4O4, C2H4O2, formula weight ¼ 534.491, crystal
˚
ꢀ
1 V. A. Zammit, L. K. Buckett, A. V. Turnbull, H. Wure and
A. Proven, Pharmacol. Ther., 2008, 118, 295.
2 B. K. Hubbard, I. Enyedy, T. A. Gilmore and M. Serrano-Wu,
Expert Opin. Ther. Pat., 2007, 17, 1331.
system ¼ triclinic, space group ¼ P1, a ¼ 5.1885(5) A, b ¼
˚
˚
11.4587(10) A, c ¼ 21.469(2) A, a ¼ 75.373(5), b ¼
3
˚
86.058(5), g ¼ 83.124(4), V ¼ 1225.2(2) A , T ¼ 200 K, Z ¼
2, Dc ¼ 1.449 Mg mꢂ3, (Mo-Ka) l ¼ 0.71073 A, m ¼ 0.12
˚
This journal is ª The Royal Society of Chemistry 2013
Med. Chem. Commun., 2013, 4, 151–158 | 157