The desoxazoline asidiacyclamide analogue cyclo(Gly–Thr–D-Val–Thz–Ile–Thr–D-Val–Thz) acetonitrile monosolvate

Asano, A.; Doi, M.

doi:10.1107/S1600536811051543

Volume 68
Part 1
Pages o54-o55
January 2012

Received 16 November 2011
Accepted 30 November 2011
Online 10 December 2011

Key indicators
Single-crystal X-ray study
T = 200 K
Mean (C-C) = 0.007 Å
Disorder in main residue
R = 0.075
wR = 0.213
Data-to-parameter ratio = 17.4
Details

The desoxazoline asidiacyclamide analogue cyclo(Gly-Thr-D-Val-Thz-Ile-Thr-D-Val-Thz) acetonitrile monosolvate

Akiko Asano ^a and Mitsunobu Doi ^a ^*

^aOsaka University of Pharmaceutical Sciences, Nasahara, Osaka 569-1094, Japan
Correspondence e-mail: doit@gly.oups.ac.jp

The title peptide [systematic name: 4-(butan-2-yl)-7,20-bis(1-hydroxyethyl)-10,23-bis(propan-2-yl)-12,25-dithia-3,6,9,16,19,22,27,28-octaazatricyclo[22.2.1.1^11,14]octacosa-1(26),11(28),13,24(27)-tetraene-2,5,8,15,18,21-hexone acetonitrile monosolvate], C₃₂H₄₈N₈O₈S₂·CH₃CN, an analogue of ascidiacyclamide (ASC) [cyclo(-Ile-Oxz-D-Val-Thz-)₂], lies about a twofold rotation axis, so that the glycine (Gly) and isoleucine (Ile) residues are each disordered over two sites with equal occupancies. The acetonitrile molecule is also located on a twofold axis passing through the C and N atoms. In the peptide, the thiazole rings are faced to each other with a dihedral angle of 9.63 (15)° and intramolecular N-HO and O-HO hydrogen bonds are observed. A bifurcated N-H(O,O) hydrogen bond links the peptide molecules into a layer parallel to the ab plane.

Related literature

For general background to ascidiacyclamide, see: Hamamoto et al. (1983); Shioiri et al. (1987); Ishida et al. (1988); Degnan et al. (1989); Doi et al. (1999); Haberhauer & Rominger (2003). For related structures, see: Schmitz et al. (1989); Asano, Doi et al. (2001); Asano, Taniguchi et al. (2001); Asano et al. (2002, 2003, 2005).

Experimental

Crystal data

C₃₂H₄₈N₈O₈S₂·C₂H₃N
M_r = 777.96
Orthorhombic, P 2₁ 2₁ 2
a = 18.2019 (9) Å
b = 10.4667 (5) Å
c = 11.0695 (6) Å
V = 2108.89 (18) Å³
Z = 2
Mo K radiation
= 0.18 mm^-1
T = 200 K
0.40 × 0.40 × 0.10 mm

Data collection

Bruker SMART APEX CCD area-detector diffractometer
Absorption correction: multi-scan (SADABS; Sheldrick, 1996) T_min = 0.909, T_max = 0.982
24275 measured reflections
4669 independent reflections
4359 reflections with I > 2(I)
R_int = 0.026

Refinement

R[F² > 2(F²)] = 0.075
wR(F²) = 0.213
S = 1.09
4669 reflections
269 parameters
H-atom parameters constrained
_max = 0.92 e Å^-3
_min = -1.42 e Å^-3
Absolute structure: Flack (1983), 2016 Friedel pairs
Flack parameter: 0.11 (13)

Table 1
Hydrogen-bond geometry (Å, °)

D-HA	D-H	HA	DA	D-HA
O22-H22O16	0.84	1.87	2.674 (4)	160
N11-H11O16ⁱ	0.88	2.12	2.984 (3)	166
N21-H21O22ⁱⁱ	0.88	2.29	2.953 (4)	132
N21-H21O24ⁱⁱ	0.88	2.25	3.013 (4)	145
N31-H31O44ⁱ	0.88	2.27	3.074 (3)	152
Symmetry codes: (i) -x+1, -y+2, z; (ii) $[-x+{\script{3\over 2}}, y-{\script{1\over 2}}, -z]$ .

Data collection: SMART (Bruker, 1998); cell refinement: SAINT-Plus (Bruker, 1998); data reduction: SAINT-Plus; program(s) used to solve structure: SHELXS97 (Sheldrick, 2008); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: PLATON (Spek, 2009); software used to prepare material for publication: SHELXL97.

Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: IS5015 ).

References

Asano, A., Doi, M., Kobayashi, K., Arimoto, M., Ishida, T., Katsuya, Y., Mezaki, Y., Hasegawa, H., Nakai, M., Sasaki, M., Taniguchi, T. & Terashima, A. (2001). Biopolymers, 58, 295-304.
Asano, A., Taniguchi, T., Sasaki, M., Hasegawa, H., Katsuya, Y. & Doi, M. (2001). Acta Cryst. E57, o834-o838.
Asano, A., Yamada, T., Katsuya, Y., Taniguchi, T., Sasaki, M. & Doi, M. (2005). J. Pept. Res. 66 (Suppl. 1), 90-98.
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Shioiri, T., Hamada, Y., Kato, S., Shibata, M., Kondo, Y., Nakagawa, H. & Kohda, K. (1987). Biochem. Pharmacol. 36, 4181-4185.
Spek, A. L. (2009). Acta Cryst. D65, 148-155.

organic compounds