Abstract
| Lingua originale | English |
|---|---|
| Numero di pagine | 118 |
| Stato di pubblicazione | Published - 2010 |
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Inactivation and polymerization of human neuroserpin. / Santangelo, Maria Grazia; Levantino, Matteo.
2010.Risultato della ricerca: Other
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TY - CONF
T1 - Inactivation and polymerization of human neuroserpin
AU - Santangelo, Maria Grazia
AU - Levantino, Matteo
PY - 2010
Y1 - 2010
N2 - Neuroserpin is an inhibitory enzyme, belonging to the family of serpins and involved in several pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). Here, we study the mechanism of neuroserpin inactivation andpolymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy, emission spectroscopy). Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. Our observations highlight the role of the different processes involved in serpin self-assembly, namely inactivating conformational changes, oligomer formation, polymer elongation and fragmentation.
AB - Neuroserpin is an inhibitory enzyme, belonging to the family of serpins and involved in several pathologies, such as ischemia, Alzheimer disease, and FENIB (Familial Encephalopathy with Neuroserpin Inclusion Body). Here, we study the mechanism of neuroserpin inactivation andpolymerization by different experimental techniques (static and dynamic light scattering, liquid chromatography, Fourier transform infrared spectroscopy, emission spectroscopy). Our results show that at intermediate temperatures (45-55 °C) neuroserpin forms flexible polymers with a size from a few tens to a few hundreds of nanometers. At high temperatures, above 80 °C, our results reveal a different polymeric form, reached through an analogous loop-sheet mechanism, with considerably larger size and higher chemical stability. Our observations highlight the role of the different processes involved in serpin self-assembly, namely inactivating conformational changes, oligomer formation, polymer elongation and fragmentation.
KW - conformational changes
KW - human neuroserpin
KW - polymerization
UR - http://hdl.handle.net/10447/52915
M3 - Other
ER -