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Review
. 2016 Nov;13(11):1609-1623.
doi: 10.1080/17425247.2016.1193149. Epub 2016 Jun 3.

Albumin nanostructures as advanced drug delivery systems

Affiliations
Review

Albumin nanostructures as advanced drug delivery systems

Mahdi Karimi et al. Expert Opin Drug Deliv. 2016 Nov.

Abstract

One of the biggest impacts that the nanotechnology has made on medicine and biology, has been in the area of drug delivery systems (DDSs). Many drugs suffer from serious problems concerning insolubility, instability in biological environments, poor uptake into cells and tissues, sub-optimal selectivity for targets and unwanted side effects. Nanocarriers can be designed as DDSs to overcome many of these drawbacks. One of the most versatile building blocks to prepare these nanocarriers is the ubiquitous, readily available and inexpensive protein, serum albumin. Areas covered: This review covers the use of different types of albumin (human, bovine, rat, and chicken egg) to prepare nanoparticle and microparticle-based structures to bind drugs. Various methods have been used to modify the albumin structure. A range of targeting ligands can be attached to the albumin that can be recognized by specific cell receptors that are expressed on target cells or tissues. Expert opinion: The particular advantages of albumin used in DDSs include ready availability, ease of chemical modification, good biocompatibility, and low immunogenicity. The regulatory approvals that have been received for several albumin-based therapeutic agents suggest that this approach will continue to be successfully explored.

Keywords: Human serum albumin; bovine serum albumin; drug delivery systems; nanoparticles; ovalbumin.

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Figures

Figure 1
Figure 1
Versatile carrier systems based on albumin NP. Different approaches for modification of albumin NPs and their application for delivery of different biomolecules are shown.
Figure 2
Figure 2
Schematic of the crystal structure of HSA and its main binding sites. Reprinted from ref [36]. with permission from John Wiley & Sons.
Figure 3
Figure 3
Desolvation based preparation of albumin nanostructure for gene/drug delivery.
Figure 4
Figure 4
(a) Scanning electron micrographs of 4T1 carcinoma spheroids, after incubation with lapatinib solution (LS) and LHNP in comparison to control group, (b) Cumulative release profile of paclitaxel from paclitaxel-BSA and paclitaxel-Chol-BSA, (c) Cellular uptake quantification of paclitaxel after incubation in MCF-7 cells for 1 h, (d) MCF-7 cell viability results after exposure to the formulations indicated, (e) Schematic illustration of the cRGD-BSA/KALA/DOX NP and their pH-triggered assembly and disassembly. (a Reproduced from ref [61]. Copyright 2015 with permission from ‘Elsevier’. b, c, d reproduced with from ref [62]. Copyright 2015 with permission from ‘Elsevier’; e reproduced from ref [63]. Copyright 2015 with permission from ‘American Chemical Society (ACS)’).
Figure 5
Figure 5
a) Schematic illustration of the composite nanoparticles composed of Au nanoclusters embedded in BSA NPs and the consequent cancer cell uptake and DOX release inducing cell death. Cellular apoptosis and related two-photon imaging are also demonstrated, b) HeLa cell viability evaluation via MTT assay after treatment with various concentrations of Au nanocluster embedded BSA NPs and DOX loaded Au nanocluster embedded BSA NPs for 36 h. Reproduced from ref [131]. Copyright 2015 with permission from John Wiley & Sons.
Figure 6
Figure 6
a) Schematic illustration of TRAIL/Dox HSA-NPs inhalation based anticancer treatment, b) Photographs of the lungs of BALB/c nu/nu mice implanted with H226 cells with and without TRAIL/Dox HSA-NPs incubation, c) Cell viability of H226 cells via MTT assay after exposure to HSA-NPs, Dox HSA-NPs (6 μg/ml), TRAIL HSA-NPs (2 μg/ml), and TRAIL/Dox HSA-NPs (6 μg/ml of Dox + 2 μg/ml of TRAIL). Reproduced from ref [37]. Copyright 2015 with permission from ‘Elsevier’.

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