NMR studies of BPTI aggregation by using paramagnetic relaxation reagents.
Paramagnetic probes, whose approach to proteins can be monitored by nuclear magnetic resonance (NMR) studies, have been found of primary relevance for investigating protein surfaces accessibility. Here, paramagnetic probes are also suggested for a systematic investigation on protein aggregation. Bovine pancreatic trypsin inhibitor (BPTI) was used as a model system for aggregation by analyzing its interaction with TEMPOL and Gd(III)DTPA-BMA. Some of the measured paramagnetic relaxation rates of BPTI protons exhibited a reverse dependence on protein concentration, which can be attributed to the formation of transient BPTI aggregates.
Bernini
Andrea
A
Biomolecular Structure Research Center and Dipartimento di Biologia Molecolare, Università di Siena, Via A. Fiorentina, I-53100 Siena, Italy.
Spiga
Ottavia
O
Ciutti
Arianna
A
Venditti
Vincenzo
V
Prischi
Filippo
F
Governatori
Mariangela
M
Bracci
Luisa
L
Lelli
Barbara
B
Pileri
Silvia
S
Botta
Mauro
M
Barge
Alessandro
A
Laschi
Franco
F
Niccolai
Neri
N
D000818:Animals; D007611:Aprotinin / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D003497:Cyclic N-Oxides; D004578:Electron Spin Resonance Spectroscopy; D019786:Gadolinium DTPA; D009682:Magnetic Resonance Spectroscopy; D008280:Magnetics; D025941:Protein Interaction Mapping; D013113:Spin Labels; D013499:Surface Properties
D003497:Cyclic N-Oxides; D013113:Spin Labels; D007611:Aprotinin; D019786:Gadolinium DTPA; C001803:tempol