Effect of temperature and loading on the structure of β-casein/ibuprofen assemblies

[Display omitted] β-Casein is a 24kDa amphiphilic and unstructured protein that self-assembles into small core–shell micelles at a wide range of concentrations, pH values and temperatures. We recently developed the micelles as nanocarriers for oral delivery of hydrophobic drugs. In this paper we exa...

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Bibliographic Details
Published in:Journal of colloid and interface science 2015-07, Vol.449, p.514-521
Main Authors: Turovsky, Tanya, Portnaya, Irina, Kesselman, Ellina, Ionita-Abutbul, Inbal, Dan, Nily, Danino, Dganit
Format: Article
Language:English
Subjects:
Animals
Anti-Inflammatory Agents, Non-Steroidal - administration & dosage
Anti-Inflammatory Agents, Non-Steroidal - chemistry
Caseins - chemistry
Cattle
Drug Carriers - chemistry
Drug-delivery
Ibuprofen - administration & dosage
Ibuprofen - chemistry
Micelles
Models, Molecular
Nanomedicine
Protein Aggregates
Protein micelles
Self-assembly
β-Casein
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Summary:[Display omitted] β-Casein is a 24kDa amphiphilic and unstructured protein that self-assembles into small core–shell micelles at a wide range of concentrations, pH values and temperatures. We recently developed the micelles as nanocarriers for oral delivery of hydrophobic drugs. In this paper we examined the effect of the hydrophobic non-steroidal anti-inflammatory drug (NSAID) ibuprofen on the micellar structure, as a function of temperature and loading. Using cryo-transmission electron microscopy (cryo-TEM) we find two routes of organization – mixed micellization and co-assembly (aggregation). The time-dependent events that characterize the second routes has been examined in detail. At 25°C we find coexistence of small assemblies and larger aggregates of irregular (but defined) structures that contain the drug. Increasing the drug loading increases the relative number of the larger aggregates and their dimensions, leading eventually to the formation of long then branched structures, like in amphiphilic block copolymer solutions. Similar trends were identified for changes in the temperature. Combined, our results suggest that ibuprofen acts as a co-surfactant that possibly is localizes to the interface rather than being encapsulated in the micellar core as other NSAID hydrophobic drugs.
ISSN:0021-9797
1095-7103
DOI:10.1016/j.jcis.2015.02.030