Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Highly potent BACE-1 protease inhibitors have been developed from an inhibitors containing a hydroxyethylene (HE) core displaying aryloxymethyl or benzyloxymethyl P1 side chain and a methoxy P1' side chain. The target molecules were synthesized in good overall yields from chiral carbohydrate starting materials. The inhibitors show high BACE-1 potency and good selectivity against cathepsin D, where the most potent inhibitor furnishes BACE-1 K(i) << 1 nM and displays >1000-fold selectivity over cathepsin D.
Design and synthesis of potent and selective BACE-1 inhibitors.,Bjorklund C, Oscarson S, Benkestock K, Borkakoti N, Jansson K, Lindberg J, Vrang L, Hallberg A, Rosenquist A, Samuelsson B J Med Chem. 2010 Feb 25;53(4):1458-64. PMID:20128595[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bjorklund C, Oscarson S, Benkestock K, Borkakoti N, Jansson K, Lindberg J, Vrang L, Hallberg A, Rosenquist A, Samuelsson B. Design and synthesis of potent and selective BACE-1 inhibitors. J Med Chem. 2010 Feb 25;53(4):1458-64. PMID:20128595 doi:10.1021/jm901168f
