Micro-heterogeneity and aggregation in β2-microglobulin solutions: Effects of temperature, pH, and conformational variant addition

Roberto Piazza, Matteo Pierno, Sara Iacopini, Palma Mangione, Gennaro Esposito, Vittorio Bellotti

Research output: Contribution to journalArticle

Abstract

We show that β2-microglobulin solutions in physiological conditions contain a tiny fraction of aggregates, which can hardly be filtered out and tend to re-form spontaneously. At physiological pH the fractional amount and size distribution of the latter aggregates do not depend on temperature. Conversely, in the pH range typical of the peri-articular tissue acidosis that often occurs in hemodialysis, temperature increase leads to fast and irreversible growth of the aggregates. Quite similar, but strongly enhanced aggregation effects can be induced even in physiological conditions by adding a very small amount of ΔN6, a naturally occurring truncated isoform of β2-m known to promote fibrillogenesis.

Original languageEnglish (US)
Pages (from-to)439-445
Number of pages7
JournalEuropean Biophysics Journal
Volume35
Issue number5
DOIs
StatePublished - May 1 2006

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Temperature
Acidosis
Renal Dialysis
Protein Isoforms
Joints
Growth

ASJC Scopus subject areas

  • Biophysics

Cite this

Micro-heterogeneity and aggregation in β2-microglobulin solutions : Effects of temperature, pH, and conformational variant addition. / Piazza, Roberto; Pierno, Matteo; Iacopini, Sara; Mangione, Palma; Esposito, Gennaro; Bellotti, Vittorio.

In: European Biophysics Journal, Vol. 35, No. 5, 01.05.2006, p. 439-445.

Research output: Contribution to journalArticle

Piazza, Roberto ; Pierno, Matteo ; Iacopini, Sara ; Mangione, Palma ; Esposito, Gennaro ; Bellotti, Vittorio. / Micro-heterogeneity and aggregation in β2-microglobulin solutions : Effects of temperature, pH, and conformational variant addition. In: European Biophysics Journal. 2006 ; Vol. 35, No. 5. pp. 439-445.
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