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Updated: Aug 30, 2026

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases
Published on: August 27, 2021
[Determination of glycyrrhizic acid binding sites by a phage display method]
T V Il'ina1, N V Fediuk, A G Bachinskiĭ
1VECTOR State Research Center of Virology and Biotechnology, Kol'tsovo, Novosibirsk Region, 630559 Russia. tilina@ngs.ru
Abstract:
Phages that expose peptides specifically interacting with glycyrrhizic acid (GA) were selected from a phage peptide library by affinity selection and ELISA. Amino acid sequence analysis of the selected peptides and human proteins with the SIM program revealed homology to tyrosine protein kinases, serine/threonine protein kinases, tyrosine phosphatases, and some receptors. Analysis of the peptide and virus protein sequences with the BLAST program showed that GA has affinity for various surface proteins of several human viruses such as HIV-1, hepatitis C virus, and herpesviruses.
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