ArticleThe protein journal2019
Investigation on Secondary Structure Alterations of Protein Drugs as an Indicator of Their Biological Activity Upon Thermal Exposure.
Article in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Advances in Food Processing Techniques for Allergenicity Reduction and Allergen Identification.Foods (Basel, Switzerland) · 2025Review
- Novel HSA-PMEMA Nanomicelles Prepared via Site-Specific In Situ Polymerization-Induced Self-Assembly for Improved Intracellular Delivery of Paclitaxel.Pharmaceutics · 2025Article
- Radiolysis of myoglobin concentrated gels by protons: specific changes in secondary structure and production of carbon monoxide.Scientific reports · 2024Article
- A Novel 3D Printing Particulate Manufacturing Technology for Encapsulation of Protein Therapeutics: Sprayed Multi Adsorbed-Droplet Reposing Technology (SMART).Bioengineering (Basel, Switzerland) · 2022Article
- Clinical progress of therapeutics and vaccines: Rising hope against COVID-19 treatment.Process biochemistry (Barking, London, England) · 2022Article
- Probing the Role of the Conserved Arg174 in Formate Dehydrogenase by Chemical Modification and Site-Directed Mutagenesis.Molecules (Basel, Switzerland) · 2021Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein drugs are important therapeutic agents however; they may degrade during formulation processing. The objective of this study was to investigate the correlation between secondary structure alterations and the retentions of biological activity of protein upon the application of thermal stress. Catalase, horseradish peroxidase and α- chymotrypsin were employed as model proteins. Each protein was heated in a solid and solution state at a temperature of 70 °C for 1 h. Attenuated total reflectance Fourier transform infrared spectroscopy, size-exclusion chromatography and biological activity assay were performed. Results showed that heat-exposure of protein solids at 70 °C caused minimum changes in secondary structure and biological activity was almost retained. However, thermal exposure of protein aqueous solution induced significant changes in the secondary structure indicated by area overlap values and caused considerable reduction in the biological activity. The changes in secondary structures were found to be in full alignment with the loss of biological activity for both protein solids as well as aqueous solutions. Catalase lost entire biological activity upon heating in the solution state. In conclusion, the findings of the present study indicate a direct correlation between protein secondary structure alterations and the retention of biological activity which can be taken into account during the development and delivery of protein drugs formulations.
Indexed as
Identifiers
31054037What OpenQuestion holds
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.