Proton-detected solid-state NMR spectroscopy of natural-abundance peptide and protein pharmaceuticals.
The natural way: A sensitive NMR spectroscopic method is developed to obtain well-resolved two-dimensional spectra ((15)N-(1)H and (13)C-(1)H) for natural-abundance (that is, without the need for isotopic enrichment) large-molecule samples, such as biopharmaceuticals. This method gives structural insights on two lyophilized aprotinin samples and three insulin samples in lyophilized, microcrystalline suspension formulation (red; see picture) and fibril (green) forms.
Zhou
Donghua H
DH
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Shah
Gautam
G
Mullen
Charles
C
Sandoz
Dennis
D
Rienstra
Chad M
CM
D007611:Aprotinin / Q000737:chemistry; D005612:Freeze Drying; D006801:Humans; D007328:Insulin / Q000737:chemistry; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D011522:Protons
D007328:Insulin; D010455:Peptides; D011506:Proteins; D011522:Protons; D007611:Aprotinin