ArticleJournal of pharmaceutical sciences2009
Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds.
Article in Journal of pharmaceutical sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed.
- Article
- Designing Formulation Strategies for Enhanced Stability of Therapeutic Peptides in Aqueous Solutions: A Review.Pharmaceutics · 2023Review
- Glycopeptide antibiotic drug stability in aqueous solution.AAPS open · 2022Review
- Biophysical and formulation studies of the Schistosoma mansoni TSP-2 extracellular domain recombinant protein, a lead vaccine candidate antigen for intestinal schistosomiasis.Human vaccines & immunotherapeutics · 2013Article
- Improving the stability of the EC1 domain of E-cadherin by thiol alkylation of the cysteine residue.International journal of pharmaceutics · 2012Article
- Multidimensional methods for the formulation of biopharmaceuticals and vaccines.Journal of pharmaceutical sciences · 2011Review
- Enhancement of drug absorption through the blood-brain barrier and inhibition of intercellular tight junction resealing by E-cadherin peptides.Molecular pharmaceutics · 2011Article
- Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.Biophysical journal · 2008Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The development of protein drugs has been hampered by difficulties in formulating them due to their inherent chemical and physical stability, which could generate problems during the late stages of development. Thus, a basic understanding of the effect of structural features on the physicochemical stability of proteins can provide fundamental solutions to the formation of proteins. In this work, the physical stability of the EC5 protein under variable pH, temperature, and ionic strength and the role of the disulfide bond on the physical stability of EC5 were evaluated. All spectroscopic measurements were integrated in empirical phase diagrams, and these diagrams showed the stable and unstable regions of EC5. The native EC5 is more stable at high than at low ionic strength in a wide pH range during temperature elevation to 70 degrees C. The empirical phase diagrams also show that the reduced EC5 has lower stability than the parent EC5. The reduced EC5 has secondary structure only at pH 3 and 4 and is unfolded at other pH values. Finally, the reduced EC5 rapidly forms a precipitate at pH 4 and 5 upon heating. In conclusion, this study shows that ionic strength and the presence of the disulfide bonds are critical for the stability of EC5.
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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.