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PubMed · 672998

Dimeric beta-cyclodextrin complexes may mimic membrane diffusion transport.

J J Stezowski·K H Jogun·E Eckle·K Bartels
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AmyloseBiological TransportCrystallographyDiffusionMembranesModels, BiologicalMolecular ConformationPhenolsPropranololThermodynamicsWaterJournal Article

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J J Stezowski, K H Jogun, E Eckle, K Bartels. 1978-08-10. Dimeric beta-cyclodextrin complexes may mimic membrane diffusion transport.. https://doi.org/10.1038/274617a0

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To study the effect of dietary sugars and starches on parameters linked to colon carcinogenesis, female Sprague-Dawley rats were fed for one month five different diets containing sucrose, glucose, fructose, cornstarch, or Hylon 7, a starch with a high amylose content. After this period, colon proliferation, assessed by [3H] thymidine incorporation in vitro, was higher (p < 0.05) in rats fed sucrose than in rats fed glucose, fructose, or cornstarch [labeling index was 7.17 +/- 0.75, 5.03 +/- 0.07, 4.55 +/- 0.72, 4.00 +/- 0.70, and 5.89 +/- 1.05 (SE) in sucrose, glucose, fructose, cornstarch, and Hylon 7 diets, respectively]. Cecal pH was lower in rats fed cornstarch and Hylon 7 than in rats fed sucrose, glucose, or fructose. Content of short-chain fatty acids (SCFAs) in the cecum was higher in rats fed Hylon 7 than in those fed glucose and fructose. In conclusion, glucose and fructose, compared with sucrose, decrease mucosal proliferation and may be considered protective factors in colon carcinogenesis, although they do not affect SCFA production and cecal pH. On the contrary, Hylon 7 does not change mucosal proliferation but increases SCFAs and lowers cecal pH, two conditions associated with a lower risk of colon cancer.

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PubMed1995

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A stereo chemical refinement of the crystalline complex between porcine pancreatic alpha-amylase and a pseudopentasaccharide from the amylostatin family has been performed through molecular mechanics calculations, using a set of parameters appropriate for protein and protein-carbohydrate interactions. The refinement provided a starting point for docking a maltopentaose moiety within the catalytic site, in the absence of water. A thorough exploration of the different orientations and conformations of maltopentaose established the sense of binding of the amylosic substrate in the amylase cleft. After optimising the geometry of the binding site, the conformations adopted by the four contiguous linkages could be rationalised by considering the environment, either hydrophobic or hydrophilic, of the different glucose moieties. Seemingly, details of the non-bonded interactions (hydrogen bonds, van der Waals and stacking interactions) that underlie this molecular recognition have been established. In particular, it was confirmed that the three acidic amino acids of the catalytic site (Asp197, Asp300 and Glu233) are close to their glucosidic target, and that there is no steric reason to propose an alteration of the 4C1 conformation of the glucose residue prior to hydrolysis. However, in the absence of water molecules, it is difficult to elucidate the details of the catalysis. Additional macroscopic information has been gained, such as the impossibility to fit a double-helical arrangement of amylose chains in the amylasic cleft. This explains why some native starches containing such motifs resist amylolytic enzymes. Tentative models involving longer amylosic chains have been elaborated, which extend our knowledge of the interaction and orientation of starch fragments in the vicinity of the hydrolytic sites.

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PubMed1995

Production and purification of active FGF2 via recombinant fusion protein.

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