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Kinetic and thermodynamic properties of MAG antagonists
Journal
Carbohydrate Research
Volume
345
Number
10
Pages / Article-Number
1348-59
Keywords
Carbohydrate mimetics, Siglecs, Myelin-associated glycoprotein (MAC), Thermodynamics of carbohydrate-protein interactions, Kinetics of carbohydrate-lectin interactions
Abstract
Paraplegia is caused by injuries of the central nervous system (CNS) and especially young people suffer from these severe consequences as, for example, the loss of motor functions. The lack of repair of the injured nerve strands originates from the inhibitory environment for axon regeneration in the CNS. Specific inhibitory proteins block the regrowth of nerve roots. One of these neurite outgrowth inhibitors is the myelin-associated glycoprotein (MAC), which is a member of the Siglec family (sialic acid-binding immunoglobulin-like lectin). In previous studies, we identified potent small molecule MAC antagonists. In this communication, we report new neuraminic acid derivatives modified in the 4- and 5-position, and the influence of various structural modifications on their kinetic and thermodynamic binding properties. (C) 2010 Elsevier Ltd. All rights reserved.
