当前位置： SCI文献检索 > JOURNAL OF BIOTECHNOLOGY期刊下所有文献 > Albumin-binding domain from Streptococcus zooepidemicus protein Zag as a novel strategy to improve the half-life of therapeutic proteins.

Albumin-binding domain from Streptococcus zooepidemicus protein Zag as a novel strategy to improve the half-life of therapeutic proteins.

Abstract：

:Recombinant antibody fragments belong to the promising class of biopharmaceuticals with high potential for future therapeutic applications. However, due to their small size they are rapidly cleared from circulation. Binding to serum proteins can be an effective approach to improve pharmacokinetic properties of short half-life molecules. Herein, we have investigated the Zag albumin-binding domain (ABD) derived from Streptococcus zooepidemicus as a novel strategy to improve the pharmacokinetic properties of therapeutic molecules. To validate our approach, the Zag ABD was fused with an anti-TNFα single-domain antibody (sdAb). Our results demonstrated that the sdAb-Zag fusion protein was highly expressed and specifically recognizes human, rat and mouse serum albumins with affinities in the nanomolar range. Moreover, data also demonstrated that the sdAb activity against the therapeutic target (TNFα) was not affected when fused with Zag ABD. Importantly, the Zag ABD increased the sdAb half-life ∼39-fold (47min for sdAb versus 31h for sdAb-Zag). These findings demonstrate that the Zag ABD fusion is a promising approach to increase the half-life of small recombinant antibodies molecules without affecting their therapeutic efficacy. Moreover, the present study strongly suggests that the Zag ABD fusion strategy can be potentially used as a universal method to improve the pharmokinetics properties of many others therapeutics proteins and peptides in order to improve their dosing schedule and clinical effects.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Cantante C,Lourenço S,Morais M,Leandro J,Gano L,Silva N,Leandro P,Serrano M,Henriques AO,Andre A,Cunha-Santos C,Fontes C,Correia JDG,Aires-da-Silva F,Goncalves J

doi

10.1016/j.jbiotec.2017.05.017

subject

Has Abstract

pub_date

2017-07-10 00:00:00

pages

23-33

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(17)30252-3

journal_volume

253

pub_type

杂志文章

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