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Crystal structure of byakangelicin (C17H18O7).
Yang Bae Kim1, Yong Ho Oh, Il Yeung Park
1College of Pharmacy, Seoul National University, Korea. ybkim@plaza.snu.ac.kr
Archives of Pharmacal Research
|July 24, 2002
Summary
The crystal structure of byakangelicin, a furanocoumarin aldose reductase inhibitor, was determined using X-ray diffraction. Two distinct molecular conformations were observed, stabilized by hydrogen bonds and van der Waals forces.
Area of Science:
- Crystallography
- Medicinal Chemistry
- Structural Biology
Background:
- Byakangelicin is a furanocoumarin derivative.
- Aldose reductase inhibitors are of therapeutic interest.
- Understanding molecular structure is key to drug design.
Purpose of the Study:
- To determine the crystal structure of byakangelicin.
- To elucidate the molecular conformation and intermolecular interactions.
- To establish the absolute configuration of byakangelicin.
Main Methods:
- X-ray diffraction analysis was employed.
- Intensity data collected using omega-2theta scan with CuK(a) radiation.
- Structure solved by direct methods and refined using full matrix least-squares to an R-value of 0.056.
Main Results:
- The crystal structure is triclinic, space group P1, with unit cell parameters a = 8.114(1), b = 10.194(1), c = 11.428(1)A, a = 111.50(1), beta= 95.57(1), gamma = 112.52(1) degrees.
- Two byakangelicin molecules with different conformations exist in the asymmetric unit.
- Intermolecular hydrogen bonds and van der Waals forces stabilize the crystal structure.
Conclusions:
- The crystal structure of byakangelicin has been successfully determined.
- The study reveals distinct molecular conformations and intermolecular interactions.
- The absolute configuration was estimated as S-form via 'Eta refinement'.