Combination of high throughput and structural screening to assess protein stability – A screening perspective

التفاصيل البيبلوغرافية
العنوان: Combination of high throughput and structural screening to assess protein stability – A screening perspective
المؤلفون: Werner Streicher, Sujata Mahapatra, Günther H.J. Peters, Allan Nørgaard, Pernille Harris, Christin Pohl, Alina Kulakova
المصدر: Pohl, C, Mahapatra, S, Kulakova, A, Streicher, W, Peters, G H J, Nørgaard, A & Harris, P 2022, ' Combination of high throughput and structural screening to assess protein stability-A screening perspective ', European Journal of Pharmaceutics and Biopharmaceutics, vol. 171 . https://doi.org/10.1016/j.ejpb.2021.08.018
European journal of pharmaceutics and biopharmaceutics 171, 1-10 (2022). doi:10.1016/j.ejpb.2021.08.018
Pohl, C, Mahapatra, S, Kulakova, A, Streicher, W, Peters, G H J, Nørgaard, A & Harris, P 2022, ' Combination of high throughput and structural screening to assess protein stability – A screening perspective ', European Journal of Pharmaceutics and Biopharmaceutics, vol. 171, pp. 1-10 . https://doi.org/10.1016/j.ejpb.2021.08.018
بيانات النشر: Deutsches Elektronen-Synchrotron, DESY, Hamburg, 2022.
سنة النشر: 2022
مصطلحات موضوعية: Computer science, High-throughput screening, Pharmaceutical Science, Automated data, Protein stability, Protein-protein interaction, X-Ray Diffraction, High throughput screening, Scattering, Small Angle, Humans, ddc:610, Throughput (business), Small-angle X-ray scattering (SAXS), business.industry, Quality assessment, Protein Stability, Proteins, Reproducibility of Results, General Medicine, Protein engineering, Automation, High-Throughput Screening Assays, Protein–protein interaction, Workflow, Drug screening, Biochemical engineering, Protein aggregation, business, Biotechnology
الوصف: European journal of pharmaceutics and biopharmaceutics 171, 1 - 10 (2022). doi:10.1016/j.ejpb.2021.08.018
High throughput screening for measuring the stability of industrially relevant proteins and their variants is necessary for quality assessment in the development process. Advances in automation, measurement time and sample consumption for many techniques allow rapid measurements with minimal amount of protein. However, many methods include automated data analysis, potentially neglecting important aspects of the protein's behavior in certain conditions. In this study we implement small angle X-ray scattering (SAXS), typically not used to assess protein behavior in industrial screening, in a high throughput screening workflow to address problems of contradicting results and reproducibility among different high throughput methods. As a case study we use the lipases of Thermomyces lanuginosus and Rhizomucor miehei, widely used industrial biocatalysts. We show that even the initial analysis of the SAXS data without performing any time-consuming modelling provide valuable information on interparticle interactions. We conclude that recent advances in automation and data processing, have enabled SAXS to be used more widely as a tool to gain in-depth knowledge highly useful for protein formulation development. This is especially relevant in light of increasing accessibility to SAXS due to the commercial availability of benchtop instruments.
Published by Elsevier, New York, NY [u.a.]
وصف الملف: application/pdf
اللغة: English
DOI: 10.3204/pubdb-2022-01737
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea860997e4adeb3ebbd6a386757edca3
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....ea860997e4adeb3ebbd6a386757edca3
قاعدة البيانات: OpenAIRE
الوصف
DOI:10.3204/pubdb-2022-01737