Premium
Design and synthesis of sialyl Lewis x mimics as E‐ and P‐selectin inhibitors
Author(s) -
Kaila Neelu,
Thomas IV Bert E.
Publication year - 2002
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/med.10018
Subject(s) - selectin , e selectin , sialyl lewis x , cell adhesion molecule , rheumatoid arthritis , epitope , chemistry , cell adhesion , immunology , p selectin , medicine , cell , biochemistry , antigen , platelet activation , platelet
The selectins are a family of cell‐adhesion proteins that mediate the rolling of leukocytes on activated endothelial cells through the recognition of the carbohydrate epitope sialyl Lewis x (sLe x ). Control of the leukocyte‐endothelial cell adhesion process may prove useful in cases where excess recruitment of leukocytes can contribute to acute diseases such as stroke and reperfusion injury and chronic diseases such as psoriasis and rheumatoid arthritis. The development of molecules that block the interactions between sLe x and the selectins has become an active area of research. In this review, we will highlight the various approaches taken toward the development of sLe x mimetics as antagonists of E‐ and P‐selectin, including the use of structural information about the selectins and their interactions with sLe x that have been revealed through the use of NMR, protein crystallography and molecular modeling. © 2002 Wiley Periodicals, Inc. Med Res Rev, 22, No. 6, 566–601, 2002; Published online in Wiley InterScience ( www.interscience.wiley.com ). DOI 10.1002/med.10018