Structural Studies on Lithocholyl-N-(2-Aminoethyl)Amide in the Solid State

Supplementary Material for

Structural studies on lithocholyl-N-(2-aminoethyl)amide in the solid state

Kari Ahonen, Babita Behera, Elina Sievänen, Arto Valkonen, Manu Lahtinen, Minna Tolonen, Reijo Kauppinen, and Erkki Kolehmainen*

EXPERIMENTAL

Liquid state NMR:Liquid state 1D and 2D NMR spectra were recorded on a Bruker Avance DRX500 NMR spectrometer equipped with a 5 mm dual BBI probehead with a z-gradient coil operating at 500.13 MHz for 1H and 125.77 MHz for 13C, respectively. The experiments were carried out at 303 K for 5% w/v sample solution in CDCl3 (99.8 %, Aldrich). The 1H NMR chemical shifts were references to the trace of CHCl3 (7.26 ppm from int. TMS) and those of 13C to CDCl3 (77.00 ppm from int. TMS).

In the 1H NMR experiments the number of scans was 8, a /2 pulse length was 6.0 s, the flip angle was 30, the recycle delay was 2 s, and 64 K data points, zero-filled to 128 K prior to FT, in time domain were collected. The 13C NMR experiments were carried out using BBO dual probehead and performed in composite pulse decoupling mode (waltz16) using a 30 flip angle. A total of 400 scans were acquired with a recycle delay of 2 s. In order to distinguish various CHn resonances, 400 scans were acquired for 13C DEPT-135 experiments using a recycle delay of 2 s and JCH of 125 Hz. All the 13C NMR spectra were processed with 1 Hz line broadening prior to FT. In the 2D PFG 1H,13C HMQC experiment /2 pulses of 6.0 and 18.0 s for 1H and 13C, respectively, were used. Three 1 ms sine gradients with a 5:3:4 ratio and a recycle delay of 2 s were used in the Bruker pulse program, hmqcgpqf. A matrix of 1 K x 1 K data points was obtained from 512 increments of 1 K data points followed by zero filling in F1 dimension prior to FT. Sine bell apodization was used in both dimensions prior to FT.

To obtain multiple bond connectivities between protons and carbons as well as protons and nitrogens PFG 1H,13C and PFG 1H,15N HMBC experiments were performed. In PFG 1H,13C HMBC experiment the gradient program and the matrix size were the same as described for the HMQC experiment above. The pulse program was the Bruker pulse program, hmbcgplpndqf. Sine bell apodization was used in both dimensions to enhance the resolution prior to FT. The evolution delay in both PFG 1H,13C and PFG 1H,15N HMBC experiments was 50 msec corresponding to 10 Hz coupling. In PFG 1H,15N HMBC the chemical shifts were referenced to the signal of an external nitromethane in a 1 mm diameter capillary inserted coaxially inside the NMR tube.

SUPPLEMENTARY FIGURES

Fig. S1 Liquid state 1H (a), {1H}-13C (b), and 13C DEPT-135 (c) NMR spectra of 1

Fig. S213C CP/MAS NMR spectra of polymorph 2 by SCP (bottom), LCPD (middle), and SCPPI (top) dephasing experiments