TY  - JOUR
A1  - Hejazi, Mahdi
A1  - Fettke, Jörg
A1  - Paris, Oskar
A1  - Steup, Martin
T1  - The two plastidial starch-related dikinases sequentially phosphorylate glucosyl residues at the surface of both the a- and b-type allomorphs of crystallized maltodextrins but the mode of action differs
N2  - In this study, two crystallized maltodextrins were generated that consist of the same oligoglucan pattern but differ strikingly in the physical order of double helices. As revealed by x-ray diffraction, they represent the highly ordered A- and B-type allomorphs. Both crystallized maltodextrins were similar in size distribution and birefringence. They were used as model substrates to study the consecutive action of the two starch-related dikinases, the glucan, water dikinase and the phosphoglucan, water dikinase. The glucan, water dikinase and the phosphoglucan, water dikinase selectively esterify glucosyl residues in the C6 and C3 positions, respectively. Recombinant glucan, water dikinase phosphorylated both allomorphs with similar rates and caused complete glucan solubilization. Soluble neutral maltodextrins inhibited the glucan, water dikinase-mediated phosphorylation of crystalline particles. Recombinant phosphoglucan, water dikinase phosphorylated both the A- and B-type allomorphs only following a prephosphorylation by the glucan, water dikinase, and the activity increased with the extent of prephosphorylation. The action of the phosphoglucan, water dikinase on the prephosphorylated A- and B-type allomorphs differed. When acting on the B-type allomorph, by far more phosphoglucans were solubilized as compared with the A type. However, with both allomorphs, the phosphoglucan, water dikinase formed significant amounts of mono-phosphorylated phosphoglucans. Thus, the enzyme is capable of acting on neutral maltodextrins. It is concluded that the actual carbohydrate substrate of the phosphoglucan, water dikinase is defined by physical rather than by chemical parameters. A model is proposed that explains, at the molecular level, the consecutive action of the two starch-related dikinases.
Y1  - 2009
UR  - http://www.plantphysiol.org/
U6  - https://doi.org/10.1104/pp.109.138750
SN  - 0032-0889
ER  - 
TY  - JOUR
A1  - Shkilnyy, Andriy
A1  - Brandt, Jessica
A1  - Mantion, Alexandre
A1  - Paris, Oskar
A1  - Schlaad, Helmut
A1  - Taubert, Andreas
T1  - Calcium phosphate with a channel-like morphology by polymer templating
N2  - Calcium phosphate mineralization from aqueous solution in the presence of organic growth modifiers has been intensely studied in the recent past. This is mostly due to potential applications of the resulting composites in the biomaterials field. Polymers in particular are efficient growth modifiers. As a result, there has been a large amount of work on polymeric growth modifiers. Interestingly, however, relatively little work has been done on polycationic additives. The current paper shows that poly(ethylene oxide)b-poly(L-lysine) block copolymers lead to an interesting morphology of calcium phosphate precipitated at room temperature and subjected to a mild heat treatment at 85 degrees C. Electron microscopy, synchrotron X-ray diffraction, and porosity analysis show that a (somewhat) porous material with channel-like features forms. Closer inspection using transmission electron microscopy shows that the channels are probably not real channels. Much rather the morphology is the result of the aggregation of ca. 100-nm-sized rodlike primary particles, which changes upon drying to exhibit the observed channel-like features. Comparison experiments conducted in the absence of polymer and with poly(ethylene oxide)-b-poly(L-glutamate) show that these features only form in the presence of the polycationic poly(L-lysine) block, suggesting a distinct interaction of the polycation with either the crystal or the phosphate ions prior to mineralization.
Y1  - 2009
UR  - http://pubs.acs.org/journal/cmatex
U6  - https://doi.org/10.1021/Cm803244z
SN  - 0897-4756
ER  -