link.springer.com10.1007/s10853... · Web viewThe extracts were pooled, washed with brine, dried...

Supplementary Materials

pH-sensitive morphological transition from nanowire to nanovesicle

of a single amino acid based water soluble molecule

Pradyot Koley and Animesh Pramanik*

Department of Chemistry, University of Calcutta, 92, A. P. C. Road, Kolkata-700 009, India

Fax: +91 33 2351 9755.

E-mail: [email protected]

Table of contents

Contents Page numbers Contents Page numbers

Fig. S1 2 Table S1 6



Fig. S4 3 Synthesis and characterization

Fig. S5 4 of the peptides 7-12

Fig. S6 4 References 12

Fig. S7 5

Fig. S8 5

1

mailto:[email protected]

Figures

100 nm

100 nm 100 nm 50 nm

100 nm

(a) (b)

(d)(c)

100 nm

20 nm

(a) (b) (c)

Fig. S1 Transmission electron microscopic images (TEM) showing (a) hollow, multilayer

vesicular structures of peptide I, and without showing distinct and credible vesicular morphology

of (b) peptide III and (c) peptide IV from neutral aqueous solution.

Average horizontal distance ~ 38 nmAverage vertical distance ~ 1.7 nm

Fig. S2 Section analysis showing the horizontal and vertical distance of peptide I vesicular

structure grown from neutral aqueous solution (1mg mL-1).

2

0.1 1 10 100 1000 100000

10

20

30

40

50

Inte

nsity

(%)

Diameter (nm)

a)

0.1 1 10 100 1000 100000

10

20

30

40

50

Inte

nsity

(%)

Diameter (nm)

b)

0.1 1 10 100 1000 100000

10

20

30

40

Inte

nsity

(%)

Diameter (nm)

c)

0.1 1 10 100 1000 100000

10

20

30

40

Inte

nsity

(%)

Diameter (nm)

d)

Fig. S3 DLS results show the well equilibrated nanostructures of (a) peptide I, (b) peptide II, (c)

peptide III, and (d) peptide IV from their aqueous solution (1mg mL-1).

200 nm

Fig. S4 TEM image showing the rupture of the nanovesicles of peptide I in presence of KCl salt.

Arrows indicate the debris of the ruptured vesicles.

3

Fig. S5 ORTEP diagram of peptide I. Thermal ellipsoids are shown at the 50% probability.

Color code: red, oxygen; blue, nitrogen; gray, carbon; light gray, hydrogen; green, fluorine.

N1

O3

O2O5

O4

N2

Fig. S6 Crystal structure shows that the individual molecules of peptide I are regularly inter-

linked through four different types of intermolecular hydrogen bonding interactions with

adjacent neighboring peptide molecules and trifluoroacetic acid molecules in an antiparallel

fashion.

4

100 nm

Fig. S7 TEM images showing the resistance of peptide I nanovesicles to enzymatic proteolysis

by proteinase K after 24 hours incubation at physiological temperature 37°C.

300 325 350 375 400 425 450 475 500 5250.0

0.1

0.2

0.3

0.4

0.5

0.6

0.7

0.8

0.9

Abs

orba

nce

(a.u

)

Wavelength (nm)

Initial CurcuminUnencapsulated Curcumin

Fig. S8 UV absorption spectra showing the initial concentration of the curcumin (red line) and

the concentration of the unencapsulated curcumin (blue line) in methanol. Corresponding

calibration curve of curcumin in methanol is reported elsewhere [S1].

5

Tables

Table S1 Crystallographic refinement details for peptide I generated from trifluoroacetic acid /

water solvent mixture.

Crystal color ColorlessChemical Formula C16 H16 N2 O3.CF3COOHFormula Weight (g) 398.34Crystal System TriclinicSpace group P-1Z 2a (Å) 9.1590 (7)b (Å) 9.6894 (8)c (Å) 11.5260 (9)α (º) 74.118 (4)β (º) 77.024 (4)γ (º) 71.971 (4)V (Å3) 924.52 (13)Collected reflections 11029 Unique reflections 4247Reflections I>2σ(I) 2289No Parameters 260R (int) 0.0405GoF 1.018R1 , wR2 [I>2 σ(I)] 0.0791, 0.2487R1 , wR2 [all data)] 0.1322, 0.3099max, min electron 0.809, -0.473density e/ Å3

Table S2 Selected backbone torsion angle (°) of peptide I

N1-C1-C2-N2 146.77 C3-C4-C5-C6 177.16

C1-C2-N2-C3 -171.97 C4-C5-C6-O1 -12.29

C2-N2-C3-C4 167.87 C4-C5-C6-O2 168.16

N2-C3-C4-C5 -177.20

6

Table S3 Intermolecular hydrogen bonding parameters of crystals of peptide I grown from

trifluoroacetic acid / water solvent mixture.

Type H…A(Ǻ) D...A(Ǻ) D-H...A(o)

N1-H1...O3a 1.945(3) 2.831(5) 173

N1-H1...O2b 1.986(3) 2.829(4) 157

N1-H1...O5c 1.858(3) 2.748(4) 178

N2-H2…O4b 1.988(4) 2.840(5) 170

Symmetry elements: a1-x, -y, 1-z; b1-x, 1-y, 1-z; c x, y, z.

Synthesis and characterization of the peptides

Synthesis and characterization of terminally protected analogues of these peptides have been

reported elsewhere [S2].

Peptide I (NH2-Phe-m-ABA-OH): At first previously reported terminally protected analogue of

the peptide Boc-Phe-m-ABA-OMe [S2] (2.0 g, 5.02 mmol) was dissolved in methanol (20 ml)

and 2N NaOH (10 ml) was added in the solution drop wise. The reaction mixture was stirred for

1 day at room temperature. The progress of the reaction was monitored by TLC. After

completion of reaction the methanol was evaporated. The residue was diluted with water and

washed with diethyl ether. The aqueous layer was cooled in an ice-bath and then neutralized by

using 2N HCl and extracted with ethyl acetate. The solvent was evaporated in vacuo to give a

waxy colorless solid (compound 1). Yield: (1.75 g, 90.67%).

Now the compound 1 (1.75g, 4.56 mmol) was dissolved in trifluoroacetic acid (8 ml) at 0°C and

stirred at room temperature. The removal of the Boc-group was monitored by TLC. After 8 h the

trifluoroacetic acid was removed under reduced pressure to afford the crude trifluoroacetate salt.

The residue was taken up in water and washed with diethyl ether. The pH of the aqueous solution

was adjusted to pH=8 with sodium bicarbonate and extracted with ethyl acetate. The extracts

were pooled, washed with brine, dried over sodium sulphate, and concentrated to solid materials

7

of peptide I that gave a positive ninhydrin test. The peptide was fully characterised by X-ray

crystallography, FT-IR and NMR studies.

Yield: 1.20 g (4.22 mmol, 93.02%). Mp=228-230 °C; IR (KBr) : 3101, 2644, 1673, 1564 cm-1; 1H NMR (300 MHz, DMSO-d6, 25°C, TMS) ppm 10.58 (s, 1H, m-ABA (2) NH); 8.09 (s, 1H,

m-ABA (2) Ha); 7.71 (d, J = 8.1 Hz, 1H, m-ABA (2) Hd); 7.64 (d, J = 7.8 Hz, 1H, m-ABA (2)

Hb); 7.42 (t, J = 7.8 Hz, 1H, m-ABA (2) Hc); 7.21-7.30 (m, 5H, Phe (1) phenyl ring protons);

4.11-4.15 (m, 1H, Phe (1) Cα Hs); 3.26-3.37 (m, 2H, Phe (1) CβHs).

13C NMR (75 MHz, DMSO-d6): ppm 167.23, 167.01, 138.13, 134.90, 131.63, 129.50(2C),

129.31, 128.62(2C), 127.29, 125.01, 123.73, 120.41, 54.52, 37.20.

1H NMR spectra of peptide I in DMSO-d6

8

13C NMR spectra of peptide I in DMSO-d6

Analogous peptides (peptide II and peptide IV) had been prepared using the same experimental

procedure with reported precursor peptide Boc-Tyr-m-ABA-OMe and Boc-Pro-m-ABA-OMe

respectively [S2], whereas peptide III (NH2-Gly-m-ABA-OH) was synthesized by literature

method [S3].

Peptide II (NH2-Tyr-m-ABA-OH):

Yield: 80.64 %. Mp=216-218 °C; IR (KBr) : 3094, 2649, 1670, 1613, 1565, 1519 cm-1; 1H NMR

(300 MHz, DMSO-d6, 25°C, TMS) ppm 10.55 (s, 1H, m-ABA (2) NH); 9.03 (s, 1H, Tyr (1)

phenyl ring OH); 8.12 (s, 1H, m-ABA (2) Ha); 7.72 (d, J = 6.6 Hz, 1H, m-ABA (2) Hd); 7.63 (d,

J = 7.2 Hz, 1H, m-ABA (2) Hb); 7.41 (t, J = 7.8 Hz, 1H, m-ABA (2) Hc); 6.95-7.02 (m, 2H, Tyr

(1) phenyl ring protons); 6.64 (br, 2H, Tyr (1) phenyl ring protons); 4.00 (br, 1H, Tyr (1) C α Hs);

2.80-2.99 (m, 2H, Tyr (1) CβHs).

13C NMR (75 MHz, chloroform-d): ppm 167.96, 167.20, 156.60, 138.30, 130.48(2C), 129.23,

127.33, 125.12, 123.60, 121.66, 118.30, 115.42(2C), 55.03, 36.79.

9

1H NMR spectra of peptide II in DMSO-d6

13C NMR spectra of peptide II in DMSO-d6

10

Peptide IV (NH2-Pro-m-ABA-OH):

Yield: 87.30 %. Mp=166-168 °C; IR (KBr) : 3086, 2578, 1675, 1595 cm -1; 1H NMR (300 MHz,

DMSO-d6, 25°C, TMS) ppm 10.79 (s, 1H, m-ABA (2) NH); 8.21 (s, 1H, m-ABA (2) Ha); 7.77

(d, J = 8.55 Hz, 1H, m-ABA (2) Hd); 7.65 (d, J = 7.5 Hz, 1H, m-ABA (2) Hb); 7.45 (t, J = 7.95

Hz, 1H, m-ABA (2) Hc); 4.33-4.38 (m, 1H, Pro (1) Cα H); 3.21-3.37 (m, 2H, Pro (1) CγHs); 2.32-

2.41 (m, 1H, Pro (1) CβHa); 1.92-2.02 (m, 3H, Pro (1) CβHb and CδHs).

13C NMR (75 MHz, DMSO-d6): ppm 167.22, 167.01, 138.40, 131.66, 129.32, 124.98, 123.68,

120.40, 59.82, 45.89, 29.61, 23.64.

1H NMR spectra of peptide IV in DMSO-d6

11

13C NMR spectra of peptide IV in DMSO-d6

References

S1. Koley P, Pramanik A (2012) Soft Matter 8:5364

S2. Koley P, Pramanik A (2011) Adv Funct Mater 21:4126

S3. Dutta A, Kar S, Frölich R, Koley P, Pramanik A (2009) ARKIVOC (ii):31

CIF files of Peptide I

data_peptideI

_audit_creation_method SHELXL-97

_chemical_name_systematic

;

?

;

12

_chemical_name_common ?

_chemical_melting_point ?

_chemical_formula_moiety ?

_chemical_formula_sum

'C18 H17 F3 N2 O5'

_chemical_formula_weight 398.34

loop_

_atom_type_symbol

_atom_type_description

_atom_type_scat_dispersion_real

_atom_type_scat_dispersion_imag

_atom_type_scat_source

'C' 'C' 0.0033 0.0016

'International Tables Vol C Tables 4.2.6.8 and 6.1.1.4'

'H' 'H' 0.0000 0.0000


'N' 'N' 0.0061 0.0033


'O' 'O' 0.0106 0.0060


'F' 'F' 0.0171 0.0103


_symmetry_cell_setting 'Triclinic'

13

_symmetry_space_group_name_H-M 'P-1'

loop_

_symmetry_equiv_pos_as_xyz

'x, y, z'

'-x, -y, -z'

_cell_length_a 9.1590(7)

_cell_length_b 9.6894(8)

_cell_length_c 11.5260(9)

_cell_angle_alpha 74.118(4)

_cell_angle_beta 77.024(4)

_cell_angle_gamma 71.971(4)

_cell_volume 924.52(13)

_cell_formula_units_Z 2

_cell_measurement_temperature 296(2)

_cell_measurement_reflns_used 1264

_cell_measurement_theta_min 2.60

_cell_measurement_theta_max 21.51

_exptl_crystal_description needle

_exptl_crystal_colour white

_exptl_crystal_size_max 0.22

_exptl_crystal_size_mid 0.03

_exptl_crystal_size_min 0.03

14

_exptl_crystal_density_meas ?

_exptl_crystal_density_diffrn 1.435

_exptl_crystal_density_method 'not measured'

_exptl_crystal_F_000 414

_exptl_absorpt_coefficient_mu 0.124

_exptl_absorpt_correction_type 'none'

_exptl_absorpt_correction_T_min 0.973

_exptl_absorpt_correction_T_max 0.996

_exptl_absorpt_process_details ?

_exptl_special_details

;

?

;

_diffrn_ambient_temperature 296(2)

_diffrn_radiation_wavelength 0.71073

_diffrn_radiation_type MoK\a

_diffrn_radiation_source 'fine-focus sealed wire'

_diffrn_radiation_monochromator graphite

_diffrn_measurement_device_type 'Bruker APEX-II CCD'

_diffrn_measurement_method '\f and \w scans'

_diffrn_standards_interval_count 'n/a'

_diffrn_standards_interval_time 'n/a'

_diffrn_standards_decay_% 'n/a'

15

_diffrn_detector_area_resol_mean ?

_diffrn_reflns_number 11029

_diffrn_reflns_av_R_equivalents 0.0405

_diffrn_reflns_av_sigmaI/netI 0.0477

_diffrn_reflns_limit_h_min -11

_diffrn_reflns_limit_h_max 11

_diffrn_reflns_limit_k_min -12

_diffrn_reflns_limit_k_max 11

_diffrn_reflns_limit_l_min -14

_diffrn_reflns_limit_l_max 15

_diffrn_reflns_theta_min 1.86

_diffrn_reflns_theta_max 27.70

_reflns_number_total 4247

_reflns_number_gt 2289

_reflns_threshold_expression >2sigma(I)

_computing_data_collection 'Bruker APEX2'

_computing_cell_refinement 'Bruker SAINT'

_computing_data_reduction 'Bruker SAINT'

_computing_structure_solution 'SHELXS-97 (Sheldrick, 2008)'

_computing_structure_refinement 'SHELXL-97 (Sheldrick, 2008)'

_computing_molecular_graphics 'Bruker SHELXTL'

_computing_publication_material 'Bruker SHELXTL'

_refine_special_details

16

;

Refinement of F^2^ against ALL reflections. The weighted R-factor wR and

goodness of fit S are based on F^2^, conventional R-factors R are based

on F, with F set to zero for negative F^2^. The threshold expression of

F^2^ > 2sigma(F^2^) is used only for calculating R-factors(gt) etc. and is

not relevant to the choice of reflections for refinement. R-factors based

on F^2^ are statistically about twice as large as those based on F, and R-

factors based on ALL data will be even larger.

;

_refine_ls_structure_factor_coef Fsqd

_refine_ls_matrix_type full

_refine_ls_weighting_scheme calc

_refine_ls_weighting_details

'calc w=1/[\s^2^(Fo^2^)+(0.2000P)^2^+0.0000P] where P=(Fo^2^+2Fc^2^)/3'

_atom_sites_solution_primary direct

_atom_sites_solution_secondary difmap

_atom_sites_solution_hydrogens geom

_refine_ls_hydrogen_treatment mixed

_refine_ls_extinction_method SHELXL

_refine_ls_extinction_coef 0.019(10)

_refine_ls_extinction_expression

'Fc^*^=kFc[1+0.001xFc^2^\l^3^/sin(2\q)]^-1/4^'

_refine_ls_number_reflns 4247

_refine_ls_number_parameters 260

17

_refine_ls_number_restraints 0

_refine_ls_R_factor_all 0.1322

_refine_ls_R_factor_gt 0.0791

_refine_ls_wR_factor_ref 0.3099

_refine_ls_wR_factor_gt 0.2487

_refine_ls_goodness_of_fit_ref 1.018

_refine_ls_restrained_S_all 1.018

_refine_ls_shift/su_max 0.000

_refine_ls_shift/su_mean 0.000

loop_

_atom_site_label

_atom_site_type_symbol

_atom_site_fract_x

_atom_site_fract_y

_atom_site_fract_z

_atom_site_U_iso_or_equiv

_atom_site_adp_type

_atom_site_occupancy

_atom_site_symmetry_multiplicity

_atom_site_calc_flag

_atom_site_refinement_flags

_atom_site_disorder_assembly

_atom_site_disorder_group

F1 F 0.6019(7) 0.9274(9) 0.5963(4) 0.265(4) Uani 1 1 d . . .

18

F2 F 0.8348(6) 0.8425(6) 0.5795(3) 0.194(2) Uani 1 1 d . . .

O1 O 0.7504(4) 0.7250(3) 0.8095(3) 0.0962(10) Uani 1 1 d . . .

O2 O 0.6341(4) 0.9509(3) 0.8373(3) 0.0907(9) Uani 1 1 d . . .

O3 O 1.1167(3) -0.4522(3) 1.2352(2) 0.0694(7) Uani 1 1 d . . .

H3 H 1.1340 -0.5419 1.2411 0.104 Uiso 1 1 calc R . .

O4 O 0.9456(3) -0.4424(3) 1.1208(2) 0.0740(7) Uani 1 1 d . . .

O5 O 0.6061(3) 0.3292(3) 1.0448(3) 0.0791(8) Uani 1 1 d . . .

N1 N 0.6900(3) 0.1042(3) 0.9936(2) 0.0540(7) Uani 1 1 d . . .

H1 H 0.6838 0.0586 0.9412 0.065 Uiso 1 1 calc R . .

C16 C 0.8519(3) -0.1276(3) 1.0822(3) 0.0508(7) Uani 1 1 d . . .

C1 C 0.6980(4) 0.8593(4) 0.7753(3) 0.0602(8) Uani 1 1 d . . .

C2 C 0.7138(7) 0.9141(5) 0.6396(4) 0.0949(14) Uani 1 1 d . . .

F3 F 0.7290(11) 1.0460(6) 0.6070(5) 0.257(4) Uani 1 1 d . . .

C4 C 0.1916(6) 0.5613(9) 0.5436(4) 0.115(2) Uani 1 1 d . . .

H4 H 0.1123 0.6016 0.4961 0.138 Uiso 1 1 calc R . .

C5 C 0.2395(6) 0.6511(6) 0.5898(5) 0.1069(17) Uani 1 1 d . . .

H5 H 0.1938 0.7531 0.5737 0.128 Uiso 1 1 calc R . .

C6 C 0.3592(5) 0.5899(5) 0.6627(4) 0.0824(11) Uani 1 1 d . . .

H6 H 0.3933 0.6518 0.6934 0.099 Uiso 1 1 calc R . .

C7 C 0.4251(4) 0.4397(4) 0.6880(3) 0.0628(9) Uani 1 1 d . . .

C8 C 0.5472(4) 0.3716(4) 0.7712(3) 0.0695(9) Uani 1 1 d . . .

H8A H 0.5884 0.4490 0.7790 0.083 Uiso 1 1 calc R . .

H8B H 0.6320 0.3000 0.7348 0.083 Uiso 1 1 calc R . .

C9 C 0.4829(4) 0.2943(3) 0.8977(3) 0.0532(7) Uani 1 1 d . . .

H9 H 0.4536 0.2081 0.8910 0.064 Uiso 1 1 calc R . .

19

C10 C 0.6001(4) 0.2430(3) 0.9861(3) 0.0542(7) Uani 1 1 d . . .

C11 C 0.7947(3) 0.0229(3) 1.0776(3) 0.0504(7) Uani 1 1 d . . .

C12 C 0.9499(3) -0.2182(3) 1.1651(3) 0.0535(7) Uani 1 1 d . . .

C13 C 1.0020(3) -0.3796(4) 1.1703(3) 0.0540(7) Uani 1 1 d . . .

C14 C 0.2574(6) 0.4157(8) 0.5659(4) 0.1016(16) Uani 1 1 d . . .

H14 H 0.2252 0.3556 0.5317 0.122 Uiso 1 1 calc R . .

C15 C 0.3727(5) 0.3512(5) 0.6388(3) 0.0808(11) Uani 1 1 d . . .

H15 H 0.4151 0.2486 0.6549 0.097 Uiso 1 1 calc R . .

N2 N 0.3442(3) 0.3981(3) 0.9511(2) 0.0536(7) Uani 1 1 d . . .

H16A H 0.3674 0.4816 0.9488 0.080 Uiso 1 1 calc R . .

H16B H 0.3147 0.3558 1.0283 0.080 Uiso 1 1 calc R . .

H16C H 0.2672 0.4191 0.9085 0.080 Uiso 1 1 calc R . .

C17 C 0.8404(5) 0.0859(4) 1.1532(3) 0.0692(9) Uani 1 1 d . . .

H17 H 0.8047 0.1877 1.1492 0.083 Uiso 1 1 calc R . .

C18 C 0.9396(5) -0.0042(4) 1.2346(4) 0.0765(11) Uani 1 1 d . . .

H18 H 0.9696 0.0380 1.2858 0.092 Uiso 1 1 calc R . .

C19 C 0.9953(4) -0.1554(4) 1.2414(3) 0.0671(9) Uani 1 1 d . . .

H19 H 1.0623 -0.2145 1.2965 0.081 Uiso 1 1 calc R . .

H11 H 0.830(4) -0.168(4) 1.027(3) 0.070(10) Uiso 1 1 d . . .

loop_

_atom_site_aniso_label

_atom_site_aniso_U_11



20




F1 0.213(5) 0.487(12) 0.110(3) -0.012(4) -0.107(3) -0.101(6)

F2 0.193(4) 0.236(5) 0.0835(19) -0.040(2) 0.008(2) 0.026(4)

O1 0.110(2) 0.0605(16) 0.0809(16) 0.0036(13) -0.0118(16) 0.0113(15)

O2 0.100(2) 0.094(2) 0.0944(18) -0.0527(17) -0.0231(16) -0.0140(17)

O3 0.0614(14) 0.0570(14) 0.0863(15) -0.0045(12) -0.0391(12) -0.0012(11)

O4 0.0741(16) 0.0594(14) 0.0895(16) -0.0205(12) -0.0392(13) 0.0033(12)

O5 0.100(2) 0.0450(12) 0.1086(19) -0.0203(12) -0.0682(16) -0.0024(12)

N1 0.0610(15) 0.0453(13) 0.0595(14) -0.0116(11) -0.0293(12) -0.0052(11)

C16 0.0489(16) 0.0516(17) 0.0528(15) -0.0097(12) -0.0175(12) -0.0093(13)

C1 0.0651(19) 0.0524(18) 0.0651(18) -0.0102(15) -0.0300(15) -0.0066(15)

C2 0.132(4) 0.068(3) 0.075(2) -0.011(2) -0.039(3) -0.001(3)

F3 0.433(11) 0.124(4) 0.148(4) 0.046(3) -0.005(5) -0.078(5)

C4 0.084(3) 0.177(6) 0.062(2) 0.020(3) -0.032(2) -0.028(4)

C5 0.094(3) 0.096(3) 0.090(3) 0.029(3) -0.025(3) -0.004(3)

C6 0.095(3) 0.067(2) 0.073(2) 0.0069(18) -0.019(2) -0.019(2)

C7 0.0545(18) 0.073(2) 0.0529(16) -0.0017(14) -0.0154(13) -0.0111(16)

C8 0.061(2) 0.076(2) 0.069(2) -0.0049(17) -0.0204(16) -0.0175(17)

C9 0.0556(17) 0.0437(15) 0.0651(17) -0.0095(13) -0.0264(14) -0.0101(13)

C10 0.0576(17) 0.0413(15) 0.0672(17) -0.0052(13) -0.0302(14) -0.0095(13)

C11 0.0459(15) 0.0517(16) 0.0544(15) -0.0106(12) -0.0197(12) -0.0064(12)

C12 0.0443(15) 0.0583(18) 0.0527(15) -0.0059(13) -0.0156(12) -0.0061(13)

C13 0.0476(16) 0.0574(18) 0.0523(15) -0.0064(13) -0.0169(12) -0.0057(13)

21

C14 0.092(3) 0.159(5) 0.066(2) -0.026(3) -0.029(2) -0.038(3)

C15 0.079(2) 0.097(3) 0.072(2) -0.029(2) -0.0203(19) -0.018(2)

N2 0.0605(15) 0.0408(13) 0.0630(14) -0.0091(11) -0.0276(12) -0.0076(11)

C17 0.080(2) 0.0537(19) 0.079(2) -0.0229(16) -0.0379(18) 0.0010(16)

C18 0.087(3) 0.069(2) 0.085(2) -0.0248(18) -0.050(2) -0.0031(19)

C19 0.065(2) 0.070(2) 0.0668(19) -0.0143(16) -0.0341(16) -0.0030(16)

_geom_special_details

;

All esds (except the esd in the dihedral angle between two l.s. planes)

are estimated using the full covariance matrix. The cell esds are taken

into account individually in the estimation of esds in distances, angles

and torsion angles; correlations between esds in cell parameters are only

used when they are defined by crystal symmetry. An approximate (isotropic)

treatment of cell esds is used for estimating esds involving l.s. planes.

;

loop_

_geom_bond_atom_site_label_1

_geom_bond_atom_site_label_2

_geom_bond_distance

_geom_bond_site_symmetry_2

_geom_bond_publ_flag

F1 C2 1.195(6) . ?

F2 C2 1.277(6) . ?

22

O1 C1 1.223(4) . ?

O2 C1 1.216(4) . ?

O3 C13 1.329(3) . ?

O3 H3 0.8200 . ?

O4 C13 1.216(4) . ?

O5 C10 1.229(4) . ?

N1 C10 1.333(4) . ?

N1 C11 1.418(4) . ?

N1 H1 0.8600 . ?

C16 C11 1.379(4) . ?

C16 C12 1.389(4) . ?

C16 H11 0.91(4) . ?

C1 C2 1.498(5) . ?

C2 F3 1.272(7) . ?

C4 C14 1.329(9) . ?

C4 C5 1.353(9) . ?

C4 H4 0.9300 . ?

C5 C6 1.413(7) . ?

C5 H5 0.9300 . ?

C6 C7 1.367(5) . ?

C6 H6 0.9300 . ?

C7 C15 1.389(5) . ?

C7 C8 1.512(5) . ?

C8 C9 1.524(5) . ?

C8 H8A 0.9700 . ?

23

C8 H8B 0.9700 . ?

C9 N2 1.484(4) . ?

C9 C10 1.524(4) . ?

C9 H9 0.9800 . ?

C11 C17 1.385(4) . ?

C12 C19 1.389(5) . ?

C12 C13 1.475(5) . ?

C14 C15 1.384(6) . ?

C14 H14 0.9300 . ?

C15 H15 0.9300 . ?

N2 H16A 0.8900 . ?

N2 H16B 0.8900 . ?

N2 H16C 0.8900 . ?

C17 C18 1.383(5) . ?

C17 H17 0.9300 . ?

C18 C19 1.380(5) . ?

C18 H18 0.9300 . ?

C19 H19 0.9300 . ?

loop_

_geom_angle_atom_site_label_1



_geom_angle

_geom_angle_site_symmetry_1

24

_geom_angle_site_symmetry_3

_geom_angle_publ_flag

C13 O3 H3 109.5 . . ?

C10 N1 C11 127.6(3) . . ?

C10 N1 H1 116.2 . . ?

C11 N1 H1 116.2 . . ?

C11 C16 C12 120.8(3) . . ?

C11 C16 H11 120(2) . . ?

C12 C16 H11 119(2) . . ?

O2 C1 O1 128.2(3) . . ?

O2 C1 C2 117.3(3) . . ?

O1 C1 C2 114.4(3) . . ?

F1 C2 F2 109.5(5) . . ?

F1 C2 F3 101.7(6) . . ?

F2 C2 F3 102.4(6) . . ?

F1 C2 C1 115.0(5) . . ?

F2 C2 C1 115.1(4) . . ?

F3 C2 C1 111.6(4) . . ?

C14 C4 C5 120.1(5) . . ?

C14 C4 H4 119.9 . . ?

C5 C4 H4 119.9 . . ?

C4 C5 C6 120.0(5) . . ?

C4 C5 H5 120.0 . . ?

C6 C5 H5 120.0 . . ?

C7 C6 C5 120.1(4) . . ?

25

C7 C6 H6 120.0 . . ?

C5 C6 H6 120.0 . . ?

C6 C7 C15 118.2(4) . . ?

C6 C7 C8 120.7(4) . . ?

C15 C7 C8 121.0(3) . . ?

C7 C8 C9 112.3(3) . . ?

C7 C8 H8A 109.1 . . ?

C9 C8 H8A 109.1 . . ?

C7 C8 H8B 109.1 . . ?

C9 C8 H8B 109.1 . . ?

H8A C8 H8B 107.9 . . ?

N2 C9 C10 106.7(2) . . ?

N2 C9 C8 110.2(3) . . ?

C10 C9 C8 112.2(3) . . ?

N2 C9 H9 109.2 . . ?

C10 C9 H9 109.2 . . ?

C8 C9 H9 109.2 . . ?

O5 C10 N1 124.7(3) . . ?

O5 C10 C9 119.4(3) . . ?

N1 C10 C9 115.9(3) . . ?

C16 C11 C17 119.7(3) . . ?

C16 C11 N1 116.4(3) . . ?

C17 C11 N1 123.9(3) . . ?

C16 C12 C19 119.5(3) . . ?

C16 C12 C13 118.7(3) . . ?

26

C19 C12 C13 121.7(3) . . ?

O4 C13 O3 122.2(3) . . ?

O4 C13 C12 123.8(3) . . ?

O3 C13 C12 114.0(3) . . ?

C4 C14 C15 121.6(5) . . ?

C4 C14 H14 119.2 . . ?

C15 C14 H14 119.2 . . ?

C14 C15 C7 119.9(5) . . ?

C14 C15 H15 120.0 . . ?

C7 C15 H15 120.0 . . ?

C9 N2 H16A 109.5 . . ?

C9 N2 H16B 109.5 . . ?

H16A N2 H16B 109.5 . . ?

C9 N2 H16C 109.5 . . ?

H16A N2 H16C 109.5 . . ?

H16B N2 H16C 109.5 . . ?

C18 C17 C11 119.3(3) . . ?

C18 C17 H17 120.3 . . ?

C11 C17 H17 120.3 . . ?

C19 C18 C17 121.4(3) . . ?

C19 C18 H18 119.3 . . ?

C17 C18 H18 119.3 . . ?

C18 C19 C12 119.1(3) . . ?

C18 C19 H19 120.4 . . ?

C12 C19 H19 120.4 . . ?

27

_diffrn_measured_fraction_theta_max 0.982

_diffrn_reflns_theta_full 27.70

_diffrn_measured_fraction_theta_full 0.982

_refine_diff_density_max 0.809

_refine_diff_density_min -0.473

_refine_diff_density_rms 0.072

28

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