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Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...
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Valency driven modulation of SDS-insulin complexation: A physicochemical study with biorelevant electrolytes.

Muhammad Ishfaq1, Nadeem Raza2, Asad Muhammad Khan1

  • 1Department of Chemistry, COMSATS University Islamabad Abbottabad Campus, Abbottabad 22060, Pakistan.

Biophysical Chemistry
|March 22, 2026
PubMed
Summary

Electrolytes, especially divalent cations like zinc and cobalt, significantly enhance the binding between sodium dodecyl sulphate (SDS) and insulin. This improves micelle formation and protein stability, crucial for biotherapeutic systems.

Keywords:
Electrolyte effectsInsulin-surfactant interactionsMicellizationSodium dodecyl sulphate (SDS)Thermodynamic analysis

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Materials Science

Background:

  • Electrolytes play active roles in biological systems, influencing molecular interactions.
  • Understanding electrolyte effects is vital for optimizing drug delivery and protein stability.

Purpose of the Study:

  • To investigate how cation valency affects the complexation of sodium dodecyl sulphate (SDS) with insulin.
  • To elucidate the impact of physiologically relevant cations (Na+, K+, Zn2+, Co2+) on micellization and protein-surfactant binding.

Main Methods:

  • Conductometric measurements to analyze specific conductance and ion sequestration.
  • Tensiometric measurements to determine critical micelle concentration (CMC) and interfacial parameters.
  • UV-Visible spectroscopy to study complex formation and binding interactions.

Main Results:

  • Divalent cations (Zn2+, Co2+) significantly enhance SDS micellization and SDS-insulin binding compared to monovalent ions.
  • Electrolyte addition reduced CMC and altered surface tension, indicating improved molecular packing.
  • Thermodynamic analysis confirmed spontaneous binding and partitioning, with Zn2+ and Co2+ showing stronger stabilization.

Conclusions:

  • Cation valency critically influences electrolyte-surfactant-protein interactions, affecting micelle formation and stability.
  • Findings provide mechanistic insights for designing electrolyte-tuned biotherapeutic systems.
  • Enhanced protein-surfactant complexation suggests improved performance and stability for biotherapeutics.