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Volume 69 
Part 4 
Pages o516-o517  
April 2013  

Received 14 January 2013
Accepted 23 February 2013
Online 9 March 2013

Key indicators
Single-crystal X-ray study
T = 293 K
Mean [sigma](C-C) = 0.007 Å
R = 0.047
wR = 0.143
Data-to-parameter ratio = 17.1
Details
Open access

Bis{(R)-1-(3-aminosulfonyl-4-methoxyphenyl)-N-[2-(2-ethoxyphenoxy)ethyl]propan-2-aminium} adipate tetrahydrate

aLek Pharmaceuticals, Sandoz Development Centre Slovenia, Verovskova 57, SI-1526 Ljubljana, Slovenia, and bFaculty of Chemistry and Chemical Technology, University of Ljubljana, Askerceva 5, SI-1000 Ljubljana, Slovenia
Correspondence e-mail: tone.meden@fkkt.uni-lj.si

The title compound, 2C20H29N2O5S+·C6H8O42-·4H2O, which was found to be optically active, is a relatively rare example of a chiral compound crystallizing in the triclinic crystal system. The dihedral angles between the phenyl rings of the cations are 60.03 (15) and 62.03 (16)°, while the C atoms of the anion are almost coplanar (r.m.s. deviation 0.085 Å) and all trans to each other. In the crystal, the components are connected by an extensive network of N-H...O and O-H...O hydrogen bonds. The sulfonamide groups link the cations into pairs via two N-H...O hydrogen bonds about the pseudo-inversion centre, leading to the formation of R22(8) rings. The anions are stacked in between four cationic pairs. Pairs of water molecules bridge the larger building units, forming hydrogen bonds with the remaining two O atoms of the anion.

Related literature

(R)-5-(2-(2-(2-Ethoxyphenoxy)ethylamino)propyl)-2-methoxybenzenesulfonamide (generic name tamsulosin) has an [alpha]-adrenergic blocking action and possesses hypotensive activity and is used mainly for the treatment of benign prostatic hyperplasia, see: Abrams et al. (1995[Abrams, P., Schulman, C. C., Vaage, S. & Wyndaele, J. (1995). Br. J. Urol. 76, 325-336.]).

[Scheme 1]

Experimental

Crystal data
  • 2C20H29N2O5S+·C6H8O42-·4H2O

  • Mr = 1035.21

  • Triclinic, P 1

  • a = 10.4595 (2) Å

  • b = 11.9020 (3) Å

  • c = 12.6423 (3) Å

  • [alpha] = 69.439 (1)°

  • [beta] = 70.466 (1)°

  • [gamma] = 67.058 (1)°

  • V = 1320.95 (5) Å3

  • Z = 1

  • Mo K[alpha] radiation

  • [mu] = 0.17 mm-1

  • T = 293 K

  • 0.25 × 0.25 × 0.20 mm

Data collection
  • Nonius KappaCCD diffractometer

  • Absorption correction: multi-scan (DENZO-SMN; Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.]) Tmin = 0.933, Tmax = 0.966

  • 26272 measured reflections

  • 10988 independent reflections

  • 8651 reflections with I > 2[sigma](I)

  • Rint = 0.030

Refinement
  • R[F2 > 2[sigma](F2)] = 0.047

  • wR(F2) = 0.143

  • S = 1.00

  • 10988 reflections

  • 641 parameters

  • 7 restraints

  • H-atom parameters constrained

  • [Delta][rho]max = 0.42 e Å-3

  • [Delta][rho]min = -0.36 e Å-3

  • Absolute structure: Flack (1983[Flack, H. D. (1983). Acta Cryst. A39, 876-881.]), 4978 Friedel pairs

  • Flack parameter: 0.10 (8)

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
N1-H1B...O21i 0.96 2.11 3.028 (5) 160
N11-H11B...O11ii 0.86 2.23 3.029 (5) 155
N2-H2C...O3W 0.96 1.84 2.755 (4) 160
N12-H12B...O1W 0.96 1.87 2.797 (4) 160
N2-H2D...O1iii 0.96 1.98 2.854 (4) 151
N12-H12A...O3iv 0.96 1.83 2.746 (4) 159
N1-H1A...O3 0.95 1.84 2.790 (5) 173
N11-H11A...O1 0.78 2.03 2.798 (6) 169
O1W-H1WB...O2Wv 0.95 1.80 2.746 (5) 174
O3W-H3WB...O4Wvi 0.96 1.82 2.747 (5) 161
O2W-H2WA...O2 0.95 1.75 2.690 (6) 175
O4W-H4WA...O4iv 0.89 1.77 2.658 (5) 175
O1W-H1WA...O24 0.90 2.33 2.899 (4) 121
O1W-H1WA...O25 0.90 2.08 2.963 (4) 165
O3W-H3WA...O14 0.92 2.39 2.920 (4) 116
O3W-H3WA...O15 0.92 2.03 2.935 (4) 166
Symmetry codes: (i) x, y-1, z; (ii) x, y+1, z; (iii) x-1, y, z; (iv) x+1, y, z; (v) x, y, z+1; (vi) x-1, y, z-1.

Data collection: COLLECT (Nonius, 1998[Nonius (1998). COLLECT. Nonius BV, Delft, The Netherlands.]); cell refinement: DENZO-SMN (Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.]); data reduction: DENZO-SMN; program(s) used to solve structure: SIR97 (Altomare et al., 1999[Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Polidori, G. & Spagna, R. (1999). J. Appl. Cryst. 32, 115-119.]); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); molecular graphics: ORTEP-3 for Windows (Farrugia, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]) and Mercury (Macrae et al., 2006[Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor, R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453-457.]); software used to prepare material for publication: publCIF (Westrip, 2010[Westrip, S. P. (2010). J. Appl. Cryst. 43, 920-925.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: LD2093 ).


Acknowledgements

The financial support of Ministry of Education, Science, Culture and Sport of the Republic of Slovenia via grant X-2000 is acknowledged.

References

Abrams, P., Schulman, C. C., Vaage, S. & Wyndaele, J. (1995). Br. J. Urol. 76, 325-336.  [CrossRef] [ChemPort] [PubMed] [ISI]
Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Polidori, G. & Spagna, R. (1999). J. Appl. Cryst. 32, 115-119.  [ISI] [CrossRef] [ChemPort] [details]
Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.  [ISI] [CrossRef] [ChemPort] [details]
Flack, H. D. (1983). Acta Cryst. A39, 876-881.  [CrossRef] [details]
Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor, R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453-457.  [ISI] [CrossRef] [ChemPort] [details]
Nonius (1998). COLLECT. Nonius BV, Delft, The Netherlands.
Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Westrip, S. P. (2010). J. Appl. Cryst. 43, 920-925.  [ISI] [CrossRef] [ChemPort] [details]


Acta Cryst (2013). E69, o516-o517   [ doi:10.1107/S1600536813005254 ]

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