a-crystallin is a protein that plays several relevant physiological roles (i.e is the major constituent of human lens or help in maintain the correct folding of several protein) all of them affected by the occurrence of aggregation. a-crystallin supramolecular aggregation, induced by generating heat-modified a-crystallin forms, has been investigated over a range of temperature between 30 C and 60 C by means of static and dynamic light scattering and atomic force microscopy. Aggregation, after the formation of first clusters or basic aggregation units, can be described as a cluster-cluster aggregation similar to that of colloidal particles. Below a temperature TC ¼ 45 C, after a large lag time needed to form the first clusters, a fast, diffusion limited, aggregation can be observed. Above TC we observe a faster lag time followed by a slow aggregation. Correspondingly the temperature dependence of aggregation rates display an abrupt discontinuity at TC . This discontinuity and the different kinetics of aggregation shed new light in the pathogenesis of the human eye lens cataract assigning a key role to the heat modified form of a-crystallin that markedly protect from aggregation preserving the transparency of the lens.

De Spirito, M., Maulucci, G., Papi, M., Missori, M., Arcovito, G., On The Mechanisms Regulating Alpha-crystallin Activity, Abstract de <<Biophysical society, 53th annual meeting>>, (Boston, 28-February 04-March 2009 ), <<BIOPHYSICAL JOURNAL>>, 2009; 2009 (Febbraio): 90-90 [http://hdl.handle.net/10807/17307]

On The Mechanisms Regulating Alpha-crystallin Activity

De Spirito, Marco;Maulucci, Giuseppe;Papi, Massimiliano;Missori, Mauro;Arcovito, Giuseppe
2009

Abstract

a-crystallin is a protein that plays several relevant physiological roles (i.e is the major constituent of human lens or help in maintain the correct folding of several protein) all of them affected by the occurrence of aggregation. a-crystallin supramolecular aggregation, induced by generating heat-modified a-crystallin forms, has been investigated over a range of temperature between 30 C and 60 C by means of static and dynamic light scattering and atomic force microscopy. Aggregation, after the formation of first clusters or basic aggregation units, can be described as a cluster-cluster aggregation similar to that of colloidal particles. Below a temperature TC ¼ 45 C, after a large lag time needed to form the first clusters, a fast, diffusion limited, aggregation can be observed. Above TC we observe a faster lag time followed by a slow aggregation. Correspondingly the temperature dependence of aggregation rates display an abrupt discontinuity at TC . This discontinuity and the different kinetics of aggregation shed new light in the pathogenesis of the human eye lens cataract assigning a key role to the heat modified form of a-crystallin that markedly protect from aggregation preserving the transparency of the lens.
Inglese
De Spirito, M., Maulucci, G., Papi, M., Missori, M., Arcovito, G., On The Mechanisms Regulating Alpha-crystallin Activity, Abstract de <<Biophysical society, 53th annual meeting>>, (Boston, 28-February 04-March 2009 ), <<BIOPHYSICAL JOURNAL>>, 2009; 2009 (Febbraio): 90-90 [http://hdl.handle.net/10807/17307]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10807/17307
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