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通过 Sortase A 和 Butelase 1 的组合进行 IgG1 的一锅双标记和 C-C 融合蛋白的制备。

One-Pot Dual Labeling of IgG 1 and Preparation of C-to-C Fusion Proteins Through a Combination of Sortase A and Butelase 1.

机构信息

Program in Cellular and Molecular Medicine , Boston Children's Hospital, Harvard Medical School , Boston , Massachussets 02115 , United States.

Department of Microbiology , Massachusetts Institute of Technology , Cambridge , Massachussets 02139 , United States.

出版信息

Bioconjug Chem. 2018 Oct 17;29(10):3245-3249. doi: 10.1021/acs.bioconjchem.8b00563. Epub 2018 Sep 21.

DOI:10.1021/acs.bioconjchem.8b00563
PMID:30231608
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6429940/
Abstract

Site-specific chemical modification of proteins can assist in the study of their function. Furthermore, these methods are essential to develop biologicals for diagnostic and therapeutic use. Standard protein engineering protocols and recombinant expression enable the production of proteins with short peptide tags recognized by enzymes capable of site-specific modification. We report here the application of two enzymes of orthogonal specificity, sortase A and butelase 1, to prepare non-natural C-to-C fusion proteins. Using these enzymes, we further demonstrate site-selective installation of different chemical moieties at two sites in a full-size antibody molecule.

摘要

蛋白质的定点化学修饰可以辅助其功能研究。此外，这些方法对于开发用于诊断和治疗的生物制剂也至关重要。标准的蛋白质工程方案和重组表达使带有短肽标签的蛋白质得以生产，这些标签可被能够进行定点修饰的酶识别。我们在此报告了两种正交特异性酶（即 sortase A 和 butelase 1）在制备非天然 C-C 融合蛋白中的应用。利用这些酶，我们进一步在一个完整抗体分子的两个位点展示了化学基团的位点选择性连接。

相似文献

[1]
One-Pot Dual Labeling of IgG 1 and Preparation of C-to-C Fusion Proteins Through a Combination of Sortase A and Butelase 1.

Bioconjug Chem. 2018-9-21

[2]
Production of unnaturally linked chimeric proteins using a combination of sortase-catalyzed transpeptidation and click chemistry.

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[3]
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[4]
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[5]
Making and breaking peptide bonds: protein engineering using sortase.

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[6]
Site-specific N-terminal labeling of proteins using sortase-mediated reactions.

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[7]
Engineering Antibodies with C-Terminal Sortase-Mediated Modification for Targeted Nanomedicine.

Methods Mol Biol. 2019

[8]
Site-specific labeling of proteins via sortase: protocols for the molecular biologist.

Methods Mol Biol. 2015

[9]
Site-specific protein labeling with amine-containing molecules using Lactobacillus plantarum sortase.

Biotechnol J. 2011-11-7

[10]
Sortase-mediated ligations for the site-specific modification of proteins.

Curr Opin Chem Biol. 2014-10-6

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[3]
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[4]
Homogeneous multi-payload antibody-drug conjugates.

Nat Chem. 2024-6

[5]
Optimized Production of Fc Fusion Proteins by Sortase Enzymatic Ligation.

Ind Eng Chem Res. 2021-12-1

[6]
Tertiary amide bond formation by an engineered asparaginyl ligase.

Chem Sci. 2024-3-5

[7]
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[8]
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Cancer Gene Ther. 2024-1

[9]
The Evolving Landscape of Antibody-Drug Conjugates: In Depth Analysis of Recent Research Progress.

Bioconjug Chem. 2023-11-15

[10]
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本文引用的文献

[1]
Total chemical synthesis of photoactivatable proteins for light-controlled manipulation of antigen-antibody interactions.

Chem Sci. 2016-3-1

[2]
Chemical Synthesis of the Highly Hydrophobic Antiviral Membrane-Associated Protein IFITM3 and Modified Variants.

Angew Chem Int Ed Engl. 2017-9-7

[3]
Enzymatic Engineering of Live Bacterial Cell Surfaces Using Butelase 1.

Angew Chem Int Ed Engl. 2017-6-9

[4]
Chemical synthesis of dual labeled proteins via differently protected alkynes enables intramolecular FRET analysis.

Chem Commun (Camb). 2017-5-30

[5]
Hepta-Mutant Staphylococcus aureus Sortase A (SrtA) as a Tool for in Vivo Protein Labeling in Caenorhabditis elegans.

ACS Chem Biol. 2017-3-17

[6]
Butelase-mediated cyclization and ligation of peptides and proteins.

Nat Protoc. 2016-10

[7]
Butelase-Mediated Macrocyclization of d-Amino-Acid-Containing Peptides.

Angew Chem Int Ed Engl. 2016-9-14

[8]
Recent advances in sortase-catalyzed ligation methodology.

Curr Opin Struct Biol. 2016-6

[9]
Total Synthesis of Circular Bacteriocins by Butelase 1.

J Am Chem Soc. 2016-5-27

[10]
Chemical Synthesis of Phosphorylated Histone H2A at Tyr57 Reveals Insight into the Inhibition Mode of the SAGA Deubiquitinating Module.

Angew Chem Int Ed Engl. 2016-4-11

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