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Fusion Protein Linkers: Property, Design and Functionality - PMC
Source: ncbi.nlm.nih.gov
Article summary:
1. This review covers the current knowledge of fusion protein linkers and summarizes examples for their design and application.
2. Linkers may offer many advantages for the production of fusion proteins, such as improving biological activity, increasing expression yield, and achieving desirable pharmacokinetic profiles.
3. Natural linkers mainly adopted extended conformations, and had independent structures that did not interact with the adjacent protein domains.
Article analysis:
The article “Fusion Protein Linkers: Property, Design and Functionality” is a comprehensive review of the current knowledge on fusion protein linkers and their applications in recombinant fusion proteins. The article provides an overview of the properties of linkers derived from naturally-occurring multi-domain proteins as a general reference for linker design, followed by a discussion on empirical linkers that have been applied to successful construction of recombinant fusion proteins. Lastly, various functions that can be achieved by utilizing linkers in recombinant fusion proteins are presented.
The article is generally reliable and trustworthy due to its comprehensive coverage of the topic at hand. It presents both natural and empirical linker designs in detail, providing readers with a thorough understanding of how they can be used to construct stable, bioactive fusion proteins. Furthermore, it also provides examples of how these linkers can be used to improve biological activity, increase expression yield or alter pharmacokinetic profiles.
However, there are some potential biases in the article which should be noted. For example, while it does provide an overview of natural linker properties derived from naturally-occurring multi-domain proteins as a general reference for linker design, it does not explore other possible sources or methods for designing effective empirical linkers. Additionally, while it does discuss various functions that can be achieved by utilizing linkers in recombinant fusion proteins (e.g., improving folding/stability or altering PK profiles), it does not provide any evidence or data to support these claims or explore any potential risks associated with using these types of linkers in recombinant fusion proteins (e.g., immunogenicity).
In conclusion, this article is generally reliable and trustworthy due to its comprehensive coverage of the topic at hand; however there are some potential biases which should be noted when considering its use as a source for further research into this area.