
Serum albumin is highly important and interesting as a nanocarrier or nanoplatform for therapeutics due to several key properties:
Biocompatibility and Nonimmunogenicity: Albumin is a naturally occurring protein in blood, which minimizes immune responses and toxicity, making it safe for human use.
Abundant and Cost-Effective: It is readily available and inexpensive to produce, facilitating scalable manufacturing of albumin-based nanocarriers.
Excellent Binding Capacity: Albumin can bind a wide range of drugs, including hydrophobic and hydrophilic molecules, enhancing drug solubility and stability.
Long Circulation Time: It has a naturally long half-life in blood, which can prolong the circulation time of drug-loaded nanoparticles, improving therapeutic efficacy.
Targeting and Biodistribution: Albumin interacts with specific receptors on cell surfaces, enabling targeted delivery to tumors and other tissues.
Versatility in Functionalization: Its structure allows for surface modifications, enabling attachment of targeting ligands or imaging agents.
Potential for Controlled Release: Albumin-based nanoparticles can be engineered to release therapeutics in response to specific stimuli, improving drug delivery precision.
In the paper, “Preparation of bovine serum albumin nanospheres via desolvation: a study of synthesis, characterization, and aging,” researchers found a desolvation procedure that is an effective and consistent method of albumin nanoparticle synthesis.
Part of the work involved the determination of size, monodispersity and zeta potential of the nanoparticles via dynamic light scattering and electrophoretic light scattering using the Brookhaven Instruments NanoBrook Omni instrument to predict colloidal stability.
The optimization steps taken by this study yielded glucose-crosslinked BSA nanoparticles with a stability exceeding that reported in previous literature.
This research points to a path of further exploration for producing controlled-release and cell-targeting nanocarriers using an alternate, non-destructive method to high-pressure homogenization (HPH) which can alter the tertiary structure of the protein due to the shear forces applied during HPH nanoemulsion preparation, which can in turn lead to denaturation and decreased biological activity.
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