ReviewFrontiers in bioengineering and biotechnology2021
Coiled-Coil Based Inclusion Bodies and Their Potential Applications.
Review in Frontiers in bioengineering and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Tandem Repeat Gene Strategy for High-Yield Production and Functional Evaluation of Bioactive Wheat Oligopeptides.Applied biochemistry and biotechnology · 2026Article
- Sequence-Encoded Aggregation of AA10 LPMO Domains as a Basis for Inclusion Body Design.International journal of molecular sciences · 2026Article
- Protein Nanoparticles for Targeted SARS-CoV-2 Trapping and Neutralization.Advanced healthcare materials · 2025Article
- Building Up Functional Coiled-Coil-Based Supramolecular Assemblies for Biomedical and Biotechnological Applications.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Magnetic protein aggregates generated by supramolecular assembly of ferritin cages - a modular strategy for the immobilization of enzymes.Frontiers in bioengineering and biotechnology · 2024Article
- Pull-Down Into Active Inclusion Bodies and Their Application in the Detection of (Poly)-Phosphates and Metal-Ions.Frontiers in bioengineering and biotechnology · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The production of recombinant proteins using microbial cell factories is frequently associated with the formation of inclusion bodies (IBs). These proteinaceous entities can be sometimes a reservoir of stable and active protein, might display good biocompatibility, and are produced efficiently and cost-effectively. Thus, these submicrometric particles are increasingly exploited as functional biomaterials for biotechnological and biomedical purposes. The fusion of aggregation-prone sequences to the target protein is a successful strategy to sequester soluble recombinant polypeptides into IBs. Traditionally, the use of these IB-tags results in the formation of amyloid-like scaffolds where the protein of interest is trapped. This amyloid conformation might compromise the protein's activity and be potentially cytotoxic. One promising alternative to overcome these limitations exploits the coiled-coil fold, composed of two or more α-helices and widely used by nature to create supramolecular assemblies. In this review, we summarize the state-of-the-art of functional IBs technology, focusing on the coiled-coil-assembly strategy, describing its advantages and applications, delving into future developments and necessary improvements in the field.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.