ArticlemAbs
Cold denaturation of monoclonal antibodies.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 63 citations in OpenAlex.
- Separation of Monoclonal Antibody Aggregates Using an Analytical Ultrafiltration Technique.Membranes · 2026Article
- The colder, the better? Sustainability in frozen storage of a monoclonal antibody drug substance.International journal of pharmaceutics: X · 2026Article
- Pharmaceutical Stability of Romiplostim: In-use Functional Study Using Microscale Thermophoresis New Strategy and Elisa.Pharmaceutical research · 2026Article
- Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry.Nature communications · 2025Article
- Membrane-based inverse-transition purification facilitates a rapid isolation of various spider-silk elastin-like polypeptide fusion proteins from extracts of transgenic tobacco.Transgenic research · 2024Article
- Isothermal chemical denaturation assay for monitoring protein stability and inhibitor interactions.Scientific reports · 2023Article
- Article
- Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.Angewandte Chemie (International ed. in English) · 2022Article
- Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- A novel method for the storage and transport of biological samples of therapeutic proteins prior to the detection of analytes using ELISA.Scientific reports · 2021Article
- Conformational Ensembles of Antibodies Determine Their Hydrophobicity.Biophysical journal · 2021Article
- Monoclonal Antibody Reagent Stability and Expiry Recommendation Combining Experimental Data with Mathematical Modeling.The AAPS journal · 2020Article
- Heavy chain dimers stabilized by disulfide bonds are required to promote in vitro assembly of trastuzumab.BMC molecular and cell biology · 2020Article
- Adapting the chemical unfolding assay for high-throughput protein screening using experimental and spectroscopic corrections.Analytical biochemistry · 2018Article
- Effects of Excipient Interactions on the State of the Freeze-Concentrate and Protein Stability.Pharmaceutical research · 2017Article
- Article
- Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins.Biochemistry · 2016Article
- Bench to Bedside: Stability Studies of GMP Produced Trastuzumab-TCMC in Support of a Clinical Trial.Pharmaceuticals (Basel, Switzerland) · 2015Article
- Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kinetics.PloS one · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The susceptibility of monoclonal antibodies (mAbs) to undergo cold denaturation remains unexplored. In this study, the phenomenon of cold denaturation was investigated for a mAb, mAb1, through thermodynamic and spectroscopic analyses. Tryptophan fluorescence and circular dichroism (CD) spectra were recorded for the guanidine hydrochloride (GuHCl)-induced unfolding of mAb1 at pH 6.3 at temperatures ranging from -5 to 50 degrees C. A three-state unfolding model incorporating the linear extrapolation method was fit to the fluorescence data to obtain an apparent free energy of unfolding, DeltaG(u), at each temperature. CD studies revealed that mAb1 exhibited polyproline II helical structure at low temperatures and at high GuHCl concentrations. The Gibbs-Helmholtz expression fit to the DeltaG(u) versus temperature data from fluorescence gave a DeltaC(p) of 8.0 kcal mol(-1) K(-1), a maximum apparent stability of 23.7 kcal mol(-1) at 18 degrees C, and an apparent cold denaturation temperature (T(CD)) of -23 degrees C. DeltaG(u) values for another mAb (mAb2) with a similar framework exhibited less stability at low temperatures, suggesting a depressed protein stability curve and a higher relative T(CD). Direct experimental evidence of the susceptibility of mAb1 and mAb2 to undergo cold denaturation in the absence of denaturant was confirmed at pH 2.5. Thus, mAbs have a potential to undergo cold denaturation at storage temperatures near -20 degrees C (pH 6.3), and this potential needs to be evaluated independently for individual mAbs.
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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.