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New PDF release: Bioorganic Chemistry: Models and Applications

By Normand Voyer (auth.), F. P. Schmidtchen (eds.)

ISBN-10: 3540677461

ISBN-13: 9783540677468

Many organic platforms nonetheless carry various very fascinating molecular houses that thus far can't be matched via manmade analogs. studying concerning the ideas and methods utilized by nature may supply entry to novel nanostructures, stronger catalysts for the functionalization of hydrocarbon compounds or may possibly allow catalytic C-C bond formation lower than environmentally benign stipulations. This quantity recapitulates the state-of-the-art in these sectors of bioorganic chemistry that, instead of mimick the average instance, goal to make use of the underlying rules for beneficial applications.

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20. Receptors 61 and 63 (but not 62) were shown to complex more tightly aromatic ammonium in chloroform, using the proposed interactions. Extensive conformational studies by CD and NMR spectroscopy confirmed that the receptor framework existed in a B-sheet conformation in which only 61 24 The Development of Peptide Nanostructure 1010 109 O ,d v t~ 108 107 06r j 105 . nPrNH 2 2 3 ~ ~~i 4 5 6 7 8 =ll H2N-(CH2)n-NH2 Fig. 19. Binding constants observed for the complexation of diamines by the bis-zincporphyrin peptide 58 (striped columns) and a mono-zincporphyrin tripeptide analog (BOC-A-Zn'porphyrinE-A-OMe) (solid columns).

They also extended their work to the development of a glucose transport system by the same strategy using a larger cyclic peptide [56]. Finally, our approach to the development of artificial ion channels is based on the alignment of six crown ethers attached to an a-helical peptidic nanostructure (69) (Fig. 24) [53, 57]. Preliminary results demonstrated that 69 adopts the 1 8~'~,~3/ 7 14 21 C-term Fig. 24. Left: u-Helix axial projection of the artificial channel 69. The position of the crown-ether residues is noted by circles.

These results illustrate again the potential of peptide nanostructures for therapeutic applications. Finally, three groups have reported the preparation of artificial enzymes with catalytic activity. Stewart and co-workers [73] incorporated a "catalytic triad" from the serine proteases into a designed four ~-helix protein (80). In their design, they incorporated one of the amino acids involved in the catalytic function at the N-terminal side of the or-helices that are linked together by their C-terminal position (Fig.

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Bioorganic Chemistry: Models and Applications by Normand Voyer (auth.), F. P. Schmidtchen (eds.)


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