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Cell-free protein expression: Making membrane protein expression no longer a challenge.
Release date:
2024-07-19
Membrane proteins, as complex functional proteins, play crucial roles in substance transport, signal transduction, energy conversion, and cell proliferation and differentiation. Given their diverse cellular functions, membrane proteins have long been a focal point across multiple research disciplines.
Currently, in drug discovery, more than half of all drug targets are membrane proteins. However, due to their unique structural characteristics, recombinant expression remains a significant challenge, for several reasons, including the following:
Membrane protein localization: The proper functioning of membrane proteins is closely linked to their accurate localization; however, maintaining their native conformation and ensuring their correct targeting and insertion into the cell membrane pose significant challenges.
Transmembrane protein hydrophobicity: Because transmembrane proteins possess hydrophobic regions that enable them to stably embed in the cell membrane, protein expression in aqueous environments often leads to misfolding or aggregation and precipitation.
Protein toxicity: When transmembrane proteins are overexpressed, hydrophobic regions can lead to the accumulation of misfolded or unfolded proteins. The buildup of these proteins in the endoplasmic reticulum activates the cellular stress response, ultimately resulting in cell death.
Low natural expression level: Some membrane proteins are expressed at very low levels in their native state, making subsequent purification and detection challenging, difficult to reproduce, and time‑consuming.
Case One
Case Study Two
Cell-free protein expression technology effectively addresses the challenges associated with the expression of membrane proteins. This approach enables in vitro transcription and translation, with a reaction system that incorporates all the essential components, substrates, and energy sources required for these processes. Moreover, we tailor the in vitro reaction conditions to suit the specific characteristics of each protein, ensuring proper expression and correct folding of the target protein. As illustrated in the figure above, in our preliminary experiments, both four‑transmembrane and seven‑transmembrane proteins were expressed using a cell‑free system; following the addition of specially formulated auxiliary reagents, soluble target proteins were recovered in the supernatant, with clearly observable yields.
Therefore, we believe that cell-free protein expression technology can help you conduct protein expression research more efficiently and rapidly.
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