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- W2087107145 abstract "Abstract Inhibition of substrate binding to maltose‐binding protein (MBP) was investigated with structurally modified maltose and maltotriose derivatives that were designed based on the X‐ray analysis of maltose and maltotriose bound to MBP. In maltose, positions 1a, 2a, 2b, 4b and 6b were modified (compounds 1 – 3 , 18a , b , 28a – c , 39 and 44 ) of which only the trivalent maltose derivatives 39 and 44 exhibited high affinity to MBP. Maltotriose modifications were carried out at position 6a and 6c (compounds 45 – 51 ). Compound 50 , possessing a 6a‐ O ‐propyl group, and compound 51 , where the 6c‐hydroxy group is replaced by bromide, showed higher affinity to MBP than the parent maltotriose. Hence, the structurally quite different compounds 39 , 50 and 51 are important lead compounds for further studies. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)" @default.
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- W2087107145 date "2008-04-01" @default.
- W2087107145 modified "2023-09-23" @default.
- W2087107145 title "Maltose and Maltotriose Derivatives as Potential Inhibitors of the Maltose-Binding Protein" @default.
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- W2087107145 doi "https://doi.org/10.1002/ejoc.200701139" @default.
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