Solubis: optimize your protein

Bioinformatics
Greet De BaetsFrederic Rousseau

Abstract

Protein aggregation is associated with a number of protein misfolding diseases and is a major concern for therapeutic proteins. Aggregation is caused by the presence of aggregation-prone regions (APRs) in the amino acid sequence of the protein. The lower the aggregation propensity of APRs and the better they are protected by native interactions within the folded structure of the protein, the more aggregation is prevented. Therefore, both the local thermodynamic stability of APRs in the native structure and their intrinsic aggregation propensity are a key parameter that needs to be optimized to prevent protein aggregation. The Solubis method presented here automates the process of carefully selecting point mutations that minimize the intrinsic aggregation propensity while improving local protein stability.

References

Aug 26, 1999·International Journal of Pharmaceutics·W Wang
Sep 14, 2004·Nature Biotechnology·Ana-Maria Fernandez-EscamillaLuis Serrano
Jun 28, 2005·Nucleic Acids Research·Joost SchymkowitzLuis Serrano
Dec 20, 2005·Journal of Molecular Biology·Frederic RousseauJoost W H Schymkowitz
Apr 21, 2011·Bioinformatics·Joost Van DurmeFrederic Rousseau

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Citations

Jun 11, 2016·Protein Engineering, Design & Selection : PEDS·Joost Van DurmeJoost Schymkowitz
Aug 2, 2016·Proteomics·Irantzu Pallarès, Salvador Ventura
Jul 10, 2019·Expert Opinion on Drug Discovery·Susanna Navarro, Salvador Ventura
Jun 9, 2017·Annual Review of Chemical and Biomolecular Engineering·Gulsum MericChristopher J Roberts
Jul 8, 2017·Current Medicinal Chemistry·Irantzu Pallarés, Salvador Ventura
Dec 22, 2020·Journal of Pharmaceutical Sciences·Pin-Kuang LaiBernhardt L Trout
Jul 24, 2018·Molecular Pharmaceutics·Marcos Gil-GarciaSalvador Ventura

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