ArticleThe protein journal2015
Insulin Fibrillization at Acidic and Physiological pH Values is Controlled by Different Molecular Mechanisms.
Article in The protein journal, 2015. 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
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Who cites it
9 citing papers in PubMed.
- Article
- Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions.International journal of molecular sciences · 2024Article
- Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform.Nature communications · 2022Article
- Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State.International journal of molecular sciences · 2022Article
- Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation.PeerJ · 2021Article
- Development and In Vitro Evaluation of Linear PEI-Shelled Heparin/Berberine Nanoparticles in Human Osteosarcoma U-2 OS Cells.Molecules (Basel, Switzerland) · 2018Article
- Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.International journal of molecular sciences · 2017Article
- Vanillin Affects Amyloid Aggregation and Non-Enzymatic Glycation in Human Insulin.Scientific reports · 2017Article
- pH Induced Conformational Transitions in the Transforming Growth Factor β-Induced Protein (TGFβIp) Associated Corneal Dystrophy Mutants.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of amyloid-like fibrils by insulin was studied at different insulin concentrations, pH and temperatures. At low pH (pH 2.5) the insulin fibrillization occurred only at high ([10 lM) peptide concentrations, whereas at physiological pH values the fibril formation is inhibited at higher insulin concentrations. The enthalpy of activation Ea of the fibril growth at pH 2.5 equals to 33 kJ/mol, which is considerably lower than 84 kJ/mol at physiological pH. The fibrillization rate of insulin decreases with increasing pH at high, 250 lM concentration, which was opposite to the pH effect observed in 2.5 lM insulin solutions. The latter effect indicates that protonation of histidine residues seems to be important for the fibrillization of monomeric insulin, whereas the pH effect at high concentration may result from off-pathway oligomerization propensity. Together, the different effect of environmental factors on the insulin fibrillization suggest that the reaction rate is controlled by different molecular events in acidic conditions and at physiological pH values.
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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.