^1H{^(19)F} NOE NMR Structural Signatures of the Insulin R_6 Hexamer: Evidence of a Capped HisB10 Site in Aryl- and Arylacryloyl-carboxylate Complexes

摘要

New and improved insulin: ^1H{^(19)F} NOE NMR difference spectra for CF_3-substituted aromatic carboxylates bound at the HisB10 sites of the R_6 human insulin (HI) hexamer show strong NOEs between the CF_3 groups and the LeuB6, AsnB3, and PheB1 sidechains. The NOEs and structural modeling establish that these carboxylates form closed complexes with the HisB10 site capped by the PheB1 rings.