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Maltose and Maltotriose Derivatives as Potential Inhibitors of the Maltose‐Binding Protein
Author(s) -
Malik Heinz,
Boos Winfried,
Schmidt Richard R.
Publication year - 2008
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200701139
Subject(s) - maltotriose , maltose , chemistry , maltose binding protein , biochemistry , substrate (aquarium) , stereochemistry , enzyme , recombinant dna , oceanography , geology , fusion protein , gene
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)