Harnessing albumin as a carrier for cancer therapies

Abstract

Serum albumin, a natural ligand carrier that is highly concentrated and long-circulating in the blood, has shown remarkable promise as a carrier for anti-cancer agents. Albumin is able to prolong the circulation half-life of otherwise rapidly cleared drugs and, importantly, promote their accumulation within tumors. The applications for using albumin as a cancer drug carrier are broad and include both traditional cancer chemotherapeutics and new classes of biologics. Strategies for leveraging albumin for drug delivery can be classified broadly into exogenous and in situ binding formulations that utilize covalent attachment, non-covalent association, or encapsulation in albumin-based nanoparticles. These methods have shown remarkable preclinical and clinical successes that are examined in this review.

An IR820 Dye–Protein Complex for Second Near‐Infrared Window and Photoacoustic Imaging

“…The previously determined crystal structure study of HSA revealed that the protein consists of three homologous domains (I‐III), and each domain has two subdomains (A and B) . Many commonly used drugs with acidic or electronegative features bind to subdomains IIA and IIIA . The docking results showed that IR820 binds to subdomain IIA of HSA (Figure a).…”

“…HSA is an abundant plasma protein in the blood and tissue fluids, and it can covalently or noncovalently attach to reporting molecules. HSA‐based probe design has shown to be a very useful and powerful strategy for developing molecular probes for theranostic treatment of diseases, especially for tumors with natural passive albumin accumulation . In this study, based on the fact that IR820 has structural similarity to ICG as well as two sulfonic acid groups, we hypothesize that it may bind to HSA, and the resulting IR820–HSA protein complex can be effectively used for NIR‐II imaging.…”

“…[33] Many commonly used drugs with acidic or electronegative features bind to subdomains IIA and IIIA. [27,34] The docking results showed that IR820 binds to subdomain IIA of HSA ( Figure 1a). As shown in the electrostatic potential map (Figure 1b), the subdomain IIA "pocket" is negatively charged and surrounded by a negatively charged outer surface.…”

“…HSA-based probe design has shown to be a very useful and powerful strategy for developing molecular probes for theranostic treatment of diseases, especially for tumors with natural passive albumin accumulation. [27][28][29] In this study, based on the fact that IR820 has structural similarity to ICG as well as two sulfonic acid groups, we hypothesize that it may bind to HSA, and the resulting IR820-HSA protein complex can be effectively used for NIR-II imaging. Moreover photoacoustic imaging (PAI) offers numerous advantages, including high spatial resolution, deeper penetration depth, and reduced optical absorption, and tissue scattering.…”

A Biocompatible Free Radical Nanogenerator with Real‐Time Monitoring Capability for High Performance Sequential Hypoxic Tumor Therapy

“…In contrast to previously reported oxygen‐irrelevant phototherapeutic agents, the present BIA NPs do not employ any inorganic/metallic carriers or photothermal agents. The use of FDA‐approved ICG and albumin‐based drug delivery systems exhibit several outstanding merits including inherent biocompatibility, long blood circulating time, and ease of mass production, showing remarkable preclinical and clinical promises …”