Cinnamomin: separation, crystallization and preliminary X-ray diffraction study.

Abstract

Cinnamomin from Cinnamonum camphora seeds, a type II ribosome-inactivating protein that interferes with protein biosynthesis in mammalian cells, can induce the apoptosis of carcinoma cells and be used as an insecticide. A rapid and improved method has been developed for the extraction and purification of cinnamomin from camphora seed. Purification of cinnamomin is achieved with two successive steps of hydrophobic interaction chromatography carried out on a fast protein liquid chromatography (FPLC) system. Crystals suitable for X-ray diffraction analysis were obtained by vapor diffusion method. A complete data set at 2.8 A resolution has been collected. Data indexation and refinement indicate that the crystal is orthorhombic with space group P2(1)2(1)2(1) and unit cell dimensions a = 52.39 A, b = 126.33 A, c = 161.45 A. There are two molecules per asymmetric unit. Initial phasing by molecular replacement method yielded a solution, which will contribute to the structure determination. A molecular model will further the understanding of the mechanism of cinnamomin function. The latter will be combined with bio-informatics to facilitate the medical and other applications of cinnamomin.

• Authors: T Wang, Y-S Zou, D-W Zhu, A Azzi, W-Y Liu, S-X Lin
• Journal: Amino acids (Amino Acids) Vol. 34 Issue 2 Pg. 239-43 (Feb 2008) ISSN: 1438-2199 [Electronic] Austria
• PMID: 17404804 (Publication Type: Journal Article)

Chemical References

• Algal Proteins
• Ribosome Inactivating Proteins, Type 2
• cinnamomin, Phytophthora cinnamomi
• Ribosome Inactivating Proteins

Topics

• Algal Proteins (chemistry, isolation & purification)
• Crystallization
• Crystallography, X-Ray
• Ribosome Inactivating Proteins (chemistry, isolation & purification)
• Ribosome Inactivating Proteins, Type 2