Colloidal carriers for intravenous drug targeting: plasma protein adsorption patterns on surface-modified latex particles evaluated by two-dimensional polyacrylamide gel electrophoresis

URN to cite this document:

urn:nbn:de:bvb:355-epub-233123 Copy

DOI to cite this document:

10.5283/epub.23312 Copy

Blunk, Torsten ; Hochstrasser, D. F. ; Sanchez, J. C. ; Müller, B. W. ; Müller, R. H.

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Date of publication of this fulltext: 27 Jan 2012 07:22

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Details

Item type:	Article
Journal or Publication Title:	Electrophoresis
Publisher:	Wiley-VCH
Volume:	14
Number of Issue or Book Chapter:	12
Page Range:	pp. 1382-1387
Date:	1993
Institutions:	Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical Technology (Prof. Göpferich)
Identification Number:	Value Type 8137807 PubMed ID
Classification:	Notation Type Adsorption MESH Apolipoproteins/analysis MESH Blood Proteins/metabolism MESH Chemistry, Physical MESH Colloids MESH Complement Factor B/analysis MESH Drug Carriers MESH Electrophoresis, Gel, Two-Dimensional MESH Fibrinogen/analysis MESH Humans MESH Injections, Intravenous MESH Microspheres MESH Physicochemical Phenomena MESH Polystyrenes/chemistry MESH Transferrin/analysis MESH
Dewey Decimal Classification:	600 Technology > 615 Pharmacy
Status:	Published
Refereed:	Yes, this version has been refereed
Created at the University of Regensburg:	Unknown
Item ID:	23312

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Abstract

Targeting to specific sites of the body via colloidal carriers is sought in order to reduce drug side effects. The adsorption of plasma proteins on intravenously injected particles is regarded as the key factor in explaining their organ distribution: total bound protein, or, more likely, the presence of specific proteins and their conformation, are expected to influence macrophage uptake. ...

Abstract

Targeting to specific sites of the body via colloidal carriers is sought in order to reduce drug side effects. The adsorption of plasma proteins on intravenously injected particles is regarded as the key factor in explaining their organ distribution: total bound protein, or, more likely, the presence of specific proteins and their conformation, are expected to influence macrophage uptake. Polystyrene beads, 60 nm in diameter, were used as model carriers; their surface was differentially modified by adsorption of increasingly hydrophilic block copolymers, poloxamers 184, 188 and 407. After incubation in plasma, the patterns of protein adsorption onto coated beads were analyzed by high-resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The behavior of some representative proteins was monitored, including albumin, fibrinogen, IgG, factor B and the apolipoproteins, A-I, A-IV, C-III, E and J. The more hydrophobic the particles, the larger the total amount of bound protein. However, this correlation was not valid for all of the analyzed protein species, which proves that it is insufficient to look only at physicochemical data to predict organ distribution. On the contrary, it is essential to use 2-D PAGE to establish the correlation between adsorbed proteins and carrier behavior in vivo.

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Metadata last modified: 26 Nov 2020 05:09

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