Premium
COMPOUNDS DESIGNED TO FIT A SITE OF KNOWN STRUCTURE IN HUMAN HAEMOGLOBIN
Author(s) -
BEDDELL C.R.,
GOODFORD P.J.,
NORRINGTON F.E.,
WILKINSON S.,
WOOTTON R.
Publication year - 1976
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1976.tb07468.x
Subject(s) - chemistry , sequence (biology) , oxygen , stereochemistry , oxygen atom , liberation , biophysics , binding site , biochemistry , molecule , biology , organic chemistry , in vitro
1 The three‐dimensional coordinates of the atoms in human haemoglobin are known, and there is a specific site in the deoxygenated form of the protein at which 2,3‐diphosphoglycerate (DPG) interacts. 2 Molecular models of this site have been constructed and used to design compounds which should bind to the deoxy conformation and stabilize it. These compounds should thereby promote oxygen liberation, as does DPG. 3 The compounds so designed were found to promote oxygen liberation. Their relative potencies, as assessed by sigmoidal dose‐response curves, are in the predicted sequence.