Issue |
Europhys. Lett.
Volume 59, Number 1, July 2002
|
|
---|---|---|
Page(s) | 149 - 154 | |
Section | Interdisciplinary physics and related areas of science and technology | |
DOI | https://doi.org/10.1209/epl/i2002-00170-7 | |
Published online | 01 June 2002 |
BLGA protein solutions at high ionic strength: Vanishing attractive interactions and “frustrated” aggregation
1
INFM, Dipartimento di Ingegneria Nucleare, Politecnico di Milano via Ponzio 34/3, 20133 Milano, Italy
2
Dipartimento di Biochimica, Università di Pavia - via
Taramelli, 27100 Pavia, Italy
Corresponding author: roberto.piazza@polimi.it
Received:
14
January
2002
Accepted:
5
April
2002
Aggregation in disperse systems is generally induced or promoted by screening of the electrostatic interactions via the addition of salts. By combining static and dynamic light scattering results from solutions of a simple milk protein, β-lactoglobulin A (BLGA), we show that clustering in protein solutions can sometimes be conversely hampered by electrolytes. This peculiar behaviour is fully correlated with a marked non-monotonic trend of the interparticle interactions as a function of the solution ionic strength. Data obtained in conditions where the protein charge has similar absolute value but opposite sign suggest that interactions depend on the specific surface charge distribution.
PACS: 87.15.Nn – Properties of solutions; aggregation and crystallization of macromolecules / 82.70.Dd – Colloids
© EDP Sciences, 2002
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.