title: Superactive insulins.
abstract: The substitution of aspartic acid for the naturally-occurring histidine residue in position B10 in human insulin results in an insulin analogue which displays an in vitro potency 4- to 5-fold greater than the parent compound. This substitution has been introduced into six insulin analogues which, before modification, display potencies ranging from less than 0.01-fold to 3-fold relative to natural insulin. In each case, the resulting aspartic acid-substituted analogue is substantially more potent than the parent compound. Thus, it is now possible to prepare "tailor-made" insulins with enhanced potency.
authors: Department of Biochemistry, Mount Sinai School of Medicine, City University of New York, New York 10029-6574.
authors: G T
authors: GT
authors: Burke
authors: S Q
authors: SQ
authors: Hu
authors: N
authors: N
authors: Ohta
authors: G P
authors: GP
authors: Schwartz
authors: L
authors: L
authors: Zong
authors: P G
authors: PG
authors: Katsoyannis
mesh_terms: D001224:Aspartic Acid / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006801:Humans; D007328:Insulin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry; D011972:Receptor, Insulin / Q000378:metabolism*
chemical_list: D007328:Insulin; D001224:Aspartic Acid; D006639:Histidine; D011972:Receptor, Insulin