ArticleThe EMBO journal1994
The affinity-selection of a minibody polypeptide inhibitor of human interleukin-6.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 65 citations in OpenAlex.
- Discovery of Antivirals Using Phage Display.Viruses · 2021Review
- Article
- The smart targeting of nanoparticles.Current pharmaceutical design · 2013Review
- In vitro selection of a peptide inhibitor of human IL-6 using mRNA display.Molecular biotechnology · 2011Article
- Directed evolution of a three-finger neurotoxin by using cDNA display yields antagonists as well as agonists of interleukin-6 receptor signaling.Molecular brain · 2011Article
- Combinatorial optimization of a CD4-mimetic miniprotein and cocrystal structures with HIV-1 gp120 envelope glycoprotein.Journal of molecular biology · 2008Article
- An improved helper phage system for efficient isolation of specific antibody molecules in phage display.Nucleic acids research · 2002Article
- Characterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoires.Journal of virology · 1997Article
- Surface topology of Minibody by selective chemical modifications and mass spectrometry.Protein science : a publication of the Protein Society · 1997Article
- Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: the case of Minibody.Protein science : a publication of the Protein Society · 1996Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A major challenge in basic and applied biological research is the engineering of small proteins with pre-determined structures and novel functions. In a limited number of cases, this has been achieved by de novo design. An alternative combinatorial approach is based on the construction of large libraries of random peptides and on methods for the selection of the desired molecules. Here we describe a successful combination of both the rational design and the combinatorial approaches for developing proteins with useful biological functions, in this case the construction of a specific inhibitor of the cytokine human interleukin-6. In previous work, the 'minibody', a 61 residue polypeptide consisting of a beta-pleated framework and two hypervariable regions, was designed, synthesized and expressed on f1 phage surface. We report the construction of a repertoire of 50 million minibodies displayed on phage in which the hypervariable regions have been randomized. One polypeptide which binds tightly and specifically to human interleukin-6 was isolated from this collection of minibody mutants. This particular minibody is an effective inhibitor of the cytokine's biological activity. The approach described here could in principle be applied to other molecular targets.
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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.