Albumin: An Emerging Opportunity in Drug Delivery
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pISSN 1226-8372 eISSN 1976-3816
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Albumin: An Emerging Opportunity in Drug Delivery Parastou Rahimizadeh, Sungtae Yang, and Sung In Lim
Received: 1 January 2020 / Revised: 25 March 2020 / Accepted: 27 March 2020 © The Korean Society for Biotechnology and Bioengineering and Springer 2020
Abstract Albumin, the most abundant and long-lived serum protein, exhibits novel features as a carrier that can greatly enhance the pharmacological action of therapeutic payloads. Besides passive trafficking by enhanced permeability and retention effect, albumin has been shown to accumulate within the tumor environment or inflamed tissues by receptor-mediated active transport, lending itself to being a promising scaffold for targeted drug delivery. Albumin has recently been found to be a scavenger for amyloid-β with the potential to treat neurodegenerative diseases. The hydrophobic binding pockets, conjugatable thiol residue, and surface-exposed N- and C-termini in albumin inherently serve as useful spots for carrying various kinds of peptidyl and non-peptidyl drugs. Beyond its long-standing role as a half-life extender, albumin is emerging as a versatile drug carrier to aid numerous therapeutic agents that have poor pharmacokinetics, targetability, solubility, and instability in vivo. Keywords: human serum albumin, drug delivery, drug carrier, conjugation, nanoparticle, fusion
1. Introduction The identification and validation of a clinically relevant target is essential for new drug discovery. By virtue of high throughput computational and experimental screening methodologies, accumulating knowledge of complex Parastou Rahimizadeh, Sung In Lim* Department of Chemical Engineering, Pukyong National University, Busan 48513, Korea Tel: +82-51-629-6435; Fax: +82-51-629-7487 E-mail: [email protected] Sungtae Yang Department of Microbiology, School of Medicine, Chosun University, Gwangju 61452, Korea
biological networks continues to reveal a multitude of novel druggable molecules. Although the expanding repertoire of newly available targets provides opportunities for drug discovery, promising drug candidates sometimes fail to proceed to clinical development due to poor biocompatibility, bioavailability, and pharmacokinetics, despite their substantial therapeutic efficacy. Therefore, in line with efforts to discover new biological targets and bioactive molecules against them, it is of great importance to implement a drug carrier that can stably deliver a therapeutic agent to a target, thereby raising the potential for advancement to clinical development. For instance, the Fc domain of immunoglobulin G (IgG) has successfully served as a fusion partner for short-lived therapeutic biomolecules for extending the serum half-lives thereof. The neonatal Fc receptor (FcRn)-binding site residing in the Fc domain interacts with FcRn receptors in a pHdependent manner [1], that rescues the Fc domain and any therapeutic entities fused or conjugated to it from lysosomal degradation upon non-specific pinocytosis, a mechanism called FcRn-m
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