Coiled-Coil Based Inclusion Bodies and Their Potential Applications

Area of Science:

• Biotechnology
• Materials Science
• Protein Engineering

Background:

• Microbial production of recombinant proteins often yields inclusion bodies (IBs).
• IBs can serve as stable, active protein reservoirs and functional biomaterials.
• Traditional methods using amyloid-like scaffolds for IB sequestration have limitations, including compromised activity and potential cytotoxicity.

Purpose of the Study:

• To review the state-of-the-art in functional inclusion bodies (IBs) technology.
• To focus on the coiled-coil assembly strategy for creating functional IBs.
• To discuss the advantages, applications, and future directions of coiled-coil-based IB technology.

Main Methods:

• Review of existing literature on inclusion body formation and functionalization.
• Analysis of strategies for protein sequestration into IBs, particularly using aggregation-prone sequences.
• Focus on the coiled-coil fold as a method for supramolecular assembly in IBs.

Main Results:

• Inclusion bodies (IBs) are increasingly utilized as functional biomaterials due to efficient, cost-effective production.
• Fusion strategies can sequester recombinant proteins into IBs, but amyloid scaffolds can reduce activity and increase toxicity.
• Coiled-coil assembly offers a promising alternative for creating functional IBs with improved properties.

Conclusions:

• Functional inclusion bodies (IBs) represent a valuable platform for biotechnological and biomedical applications.
• The coiled-coil assembly strategy provides a viable alternative to amyloid scaffolds, enhancing protein activity and biocompatibility.
• Further development and improvements in coiled-coil-based IB technology are necessary to fully exploit its potential.