NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

Andrea Bernini; Ottavia Spiga; Arianna Ciutti; Vincenzo Venditti; Filippo Prischi; Mariangela Governatori; Luisa Bracci; Barbara Lelli; Silvia Pileri; Mauro Botta; Alessandro Barge; Franco Laschi; Neri Niccolai

doi:10.1016/j.bbapap.2006.02.013

NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

Andrea Bernini, Ottavia Spiga, Arianna Ciutti, Vincenzo Venditti, Filippo Prischi, Mariangela Governatori, Luisa Bracci, Barbara Lelli, Silvia Pileri, Mauro Botta, Alessandro Barge, Franco Laschi, Neri Niccolai

Dipartimento di Scienze e Innovazione Tecnologica

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

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. Bovin 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.

Lingua originale	Inglese
pagine (da-a)	856-862
Numero di pagine	7
Rivista	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1764
Numero di pubblicazione	5
DOI	https://doi.org/10.1016/j.bbapap.2006.02.013
Stato di pubblicazione	Pubblicato - mag 2006

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10.1016/j.bbapap.2006.02.013

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@article{eac00656e19f4f54a52b7f4b3ee0601d,

title = "NMR studies of BPTI aggregation by using paramagnetic relaxation reagents",

abstract = "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. Bovin 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.",

keywords = "BPTI, Gd(III)DTPA-BMA, NMR, Paramagnetic probe, Protein aggregation, Surface accessibility, TEMPOL",

author = "Andrea Bernini and Ottavia Spiga and Arianna Ciutti and Vincenzo Venditti and Filippo Prischi and Mariangela Governatori and Luisa Bracci and Barbara Lelli and Silvia Pileri and Mauro Botta and Alessandro Barge and Franco Laschi and Neri Niccolai",

note = "Funding Information: Thanks are due to MIUR (PRIN2003-059395), and to the University of Siena for financial support. Thanks are also due to Prof. B. Halle for helpful comments. ",

year = "2006",

month = may,

doi = "10.1016/j.bbapap.2006.02.013",

language = "English",

volume = "1764",

pages = "856--862",

journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",

issn = "1570-9639",

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TY - JOUR

T1 - NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

AU - Bernini, Andrea

AU - Spiga, Ottavia

AU - Ciutti, Arianna

AU - Venditti, Vincenzo

AU - Prischi, Filippo

AU - Governatori, Mariangela

AU - Bracci, Luisa

AU - Lelli, Barbara

AU - Pileri, Silvia

AU - Botta, Mauro

AU - Barge, Alessandro

AU - Laschi, Franco

AU - Niccolai, Neri

N1 - Funding Information: Thanks are due to MIUR (PRIN2003-059395), and to the University of Siena for financial support. Thanks are also due to Prof. B. Halle for helpful comments.

PY - 2006/5

Y1 - 2006/5

N2 - 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. Bovin 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.

AB - 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. Bovin 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.

KW - BPTI

KW - Gd(III)DTPA-BMA

KW - NMR

KW - Paramagnetic probe

KW - Protein aggregation

KW - Surface accessibility

KW - TEMPOL

UR - http://www.scopus.com/inward/record.url?scp=33646507488&partnerID=8YFLogxK

U2 - 10.1016/j.bbapap.2006.02.013

DO - 10.1016/j.bbapap.2006.02.013

M3 - Article

SN - 1570-9639

VL - 1764

SP - 856

EP - 862

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

IS - 5

ER -

NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

Abstract

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