Salt Potentiates Methylamine Counteraction System to Offset the Deleterious Effects of Urea on Protein Stability and Function

Overview

Journal PLoS One

Specialties General Medicine
Science

Date 2015 Mar 21

PMID 25793733

Citations 2

Authors

Safikur Rahman

Md Tabish Rehman

Laishram R Singh

Marina Warepam

Faizan Ahmad

Tanveer Ali Dar

Affiliations

Soon will be listed here.

Abstract

Cellular methylamines are osmolytes (low molecular weight organic compounds) believed to offset the urea's harmful effects on the stability and function of proteins in mammalian kidney and marine invertebrates. Although urea and methylamines are found at 2:1 molar ratio in tissues, their opposing effects on protein structure and function have been questioned on several grounds including failure to counteraction or partial counteraction. Here we investigated the possible involvement of cellular salt, NaCl, in urea-methylamine counteraction on protein stability and function. We found that NaCl mediates methylamine counteracting system from no or partial counteraction to complete counteraction of urea's effect on protein stability and function. These conclusions were drawn from the systematic thermodynamic stability and functional activity measurements of lysozyme and RNase-A. Our results revealed that salts might be involved in protein interaction with charged osmolytes and hence in the urea-methylamine counteraction.

Citing Articles

Effect of pH on Diclofenac-Lysozyme Interaction: Structural and Functional Aspect.

Basheeruddin M, Khan S, Ahmed N, Jamal S Front Mol Biosci. 2022; 9:872905.

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Expedition into Taurine Biology: Structural Insights and Therapeutic Perspective of Taurine in Neurodegenerative Diseases.

Bhat M, Ahmad K, Khan M, Bhat M, Almatroudi A, Rahman S Biomolecules. 2020; 10(6).

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