Chemical synthesis of a 28 kDa full-length PET degrading enzyme ICCG by the removable backbone modification strategy

The combination of removable backbone modification strategy and peptide hydrazide-based native chemical ligation enables the chemical synthesis of a 28kDa full-length PET degrading enzyme ICCG (a higher depolymerization efficiency of variant leaf-branch compost cutinase (LCC)). [Display omitted] •mi...

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Published in:Bioorganic chemistry 2024-02, Vol.143, p.107047-107047, Article 107047
Main Authors: Gao, Yun-Pu, Sun, Peng-Fei, Guo, Wu-Chen, Zhou, Yong-Kang, Zheng, Ji-Shen, Tang, Shan
Format: Article
Language:English
Subjects:
Chemical protein synthesis
Hydrolases - chemistry
Peptide Fragments
Peptides - chemistry
PET-hydrolytic enzyme (PETase)
Poly(ethylene terephthalate) (PET) depolymerization
Polyethylene Terephthalates - chemistry
Removable backbone modification
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Summary:The combination of removable backbone modification strategy and peptide hydrazide-based native chemical ligation enables the chemical synthesis of a 28kDa full-length PET degrading enzyme ICCG (a higher depolymerization efficiency of variant leaf-branch compost cutinase (LCC)). [Display omitted] •mirror-image PET degrading enzyme ICCG.•Hydrazide-based chemical ligation for proteins.•Removable backbone modification for hydrophobic peptides. Chemical protein synthesis offers a powerful way to access otherwise-difficult-to-obtain proteins such as mirror-image proteins. Although a large number of proteins have been chemically synthesized to date, the acquisition to proteins containing hydrophobic peptide fragments has proven challenging. Here, we describe an approach that combines the removable backbone modification strategy and the peptide hydrazide-based native chemical ligation for the chemical synthesis of a 28 kDa full-length PET degrading enzyme IGGC (a higher depolymerization efficiency of variant leaf-branch compost cutinase (LCC)) containing hydrophobic peptide segments. The synthetic ICCG exhibits the enzymatic activity and will be useful in establishing the corresponding mirror-image version of ICCG.
ISSN:0045-2068
1090-2120
DOI:10.1016/j.bioorg.2023.107047