Human serum albumin binders: A piggyback ride for long-acting therapeutics

被引：17
作者：
Ullah, Aziz [1 ,2 ]
Shin, Goeun [1 ,4 ]
Lim, Sung In [1 ,3 ]
机构：
[1] Pukyong Natl Univ, Dept Chem Engn, Busan 48513, South Korea
[2] Gomal Univ, Fac Pharm, Gomal Ctr Pharmaceut Sci, Dera Ismail Khan 29050, Khyber Pakhtunk, Pakistan
[3] Marine BioResource Co Ltd, 365 Sinseon Ro, Busan 48548, South Korea
[4] Nbios Inc, 7 Jukheon Gil, Gangneung Si, Gangwon Do, South Korea
来源：
DRUG DISCOVERY TODAY | 2023年 / 28卷 / 10期
基金：
新加坡国家研究基金会;
关键词：
serum albumin; half-life extension; drug delivery; albumin-binding domain; long-acting therapeutics; STREPTOCOCCAL PROTEIN-G; SINGLE-CHAIN DIABODY; FATTY-ACID-BINDING; HALF-LIFE; HIGH-AFFINITY; PHARMACOKINETIC PROPERTIES; DOMAIN ANTIBODIES; CRYSTAL-STRUCTURE; FUSION PROTEIN; RECEPTOR;
D O I：
10.1016/j.drudis.2023.103738
中图分类号：
R9 [药学];
学科分类号：
1007 ;
摘要：
Human serum albumin (HSA) is the most abundant protein in the blood and has desirable properties as a drug carrier. One of the most promising ways to exploit HSA as a carrier is to append an albumin-binding moiety (ABM) to a drug for in situ HSA binding upon administration. Nature-and library-derived ABMs vary in size, affinity, and epitope, differentially improving the pharmacokinetics of an appended drug. In this review, we evaluate the current state of knowledge regarding various aspects of ABMs and the unique advantages of ABM-mediated drug delivery. Furthermore, we discuss how ABMs can be specifically modulated to maximize potential benefits in clinical development.
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页数：16
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