ArticleACS omega2022
Formation of Protamine and Zn-Insulin Assembly: Exploring Biophysical Consequences.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Dynamic Intracellular Trafficking of the Low Molecular Weight Protamine in Breast Cancer Cells.Applied biochemistry and biotechnology · 2026Article
- Comparison of subcellular trafficking of the low molecular weight protamine (LMWP) fragment in tumor and non-tumor cells.Molecular biology reports · 2026Article
- Design of Electrostatic Nanocomplex of Semaglutide with Protamine and Zinc for Subcutaneous Prolonged Delivery.Nanomaterials (Basel, Switzerland) · 2025Article
- PROTA: A Robust Tool for Protamine Prediction Using a Hybrid Approach of Machine Learning and Deep Learning.International journal of molecular sciences · 2024Article
- Design of inhibitor peptide sequences based on the interfacial knowledge of the protein G-IgG crystallographic complex and their binding studies with IgG.European biophysics journal : EBJ · 2024Article
- Computational Approach to Elucidating Insulin-Protamine Binding Interactions and Dynamics in Insulin NPH Formulations.ACS omega · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The insulin-protamine interaction is at the core of the mode of action in many insulin formulations (Zn + insulin + protamine) and to treat diabetes, in which protamine is added to the stable form of hexameric insulin (Zn-insulin). However, due to the unavailability of quantitative data and a high-resolution structure, the binding mechanism of the insulin-protamine complex remains unknown. In this study, it was observed that Zn-insulin experiences destabilization as observed by the loss of secondary structure in circular dichroism (CD), and reduction in thermal stability in melting study, upon protamine binding. In isothermal titration calorimetry (ITC), it was found that the interactions were mostly enthalpically driven. This is in line with the positive Δ
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Registered trials
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