Interaction between gastric enzyme pepsin and tetradecyltrimethylammonium bromide in presence of sodium electrolytes: Exploration of micellization behavior

Md Al Amin Hossain; Tamanna Islam; Md Tuhinur R Joy; Zannatul Kowser; Mohammad Z Ahmed; Md Tabish Rehman; Mohamed F AlAjmi; Shamim Mahbub; Md Abdul Goni; Md Anamul Hoque; Shariff E Kabir

doi:10.1016/j.ijbiomac.2023.127478

Interaction between gastric enzyme pepsin and tetradecyltrimethylammonium bromide in presence of sodium electrolytes: Exploration of micellization behavior

Int J Biol Macromol. 2023 Dec 31;253(Pt 8):127478. doi: 10.1016/j.ijbiomac.2023.127478. Epub 2023 Oct 21.

Authors

Affiliations

¹ Department of Chemistry, Jashore University of Science and Technology, Jashore 7408, Bangladesh.
² Department of Chemistry, Jashore University of Science and Technology, Jashore 7408, Bangladesh. Electronic address: joytuhinur@yahoo.com.
³ Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia. Electronic address: mahmed4@ksu.edu.sa.
⁴ Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh 11451, Saudi Arabia.
⁵ Nuclear Safety, Security & Safeguards Division, Bangladesh Atomic Energy Regulatory Authority, Agargaon, Dhaka 1207, Bangladesh.
⁶ Department of Biological and Physical Sciences, South Carolina State University, Orangeburg, SC 29117, USA.
⁷ Department of Chemistry, Jahangirnagar University, Savar, Dhaka 1342, Bangladesh.
⁸ Department of Chemistry, Jagannath University, Dhaka 1100, Bangladesh.

PMID: 37866567
DOI: 10.1016/j.ijbiomac.2023.127478

Abstract

Pepsin is a proteolytic enzyme used in the treatment of digestive disorders. In this study, we investigated the physicochemical properties of the tetradecyltrimethylammonium bromide (TTAB) and pepsin protein mixture in various sodium salt media within a temperature range of 300.55-320.55 K with 5 K intervals. The conductometric study of the TTAB+pepsin mixture revealed a reduction in the critical micelle concentration (CMC) in electrolyte media. The micellization of TTAB was delayed in the presence of pepsin. The CMC of the TTAB + pepsin mixture was found to depend on the concentrations of electrolytes and protein, as well as the temperature variations. The aggregation of the TTAB+pepsin mixture was hindered as a function of [pepsin] and increasing temperatures, while micellization was promoted in aqueous electrolyte solutions. The negative free energy changes (∆G_m⁰) indicated the spontaneous aggregation of the TTAB+pepsin mixture. Changes in enthalpy, entropy, molar heat capacities, transfer properties, and enthalpy-entropy compensation variables were calculated and illustrated rationally. The interaction forces between TTAB and pepsin protein in the experimental solvents were primarily hydrophobic and electrostatic (ion-dipole) in nature. An analysis of molecular docking revealed hydrophobic interactions as the main stabilizing forces in the TTAB-pepsin complex.

Keywords: Interaction forces; Micelles; Pepsin.

MeSH terms

Micelles
Molecular Docking Simulation
Pepsin A*
Sodium*
Water / chemistry

Substances

tetradecyltrimethylammonium
Pepsin A
Sodium
Water
Micelles