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Role of structural specificity of ZnO particles in preserving functionality of proteins in their corona.

ABSTRACT: Reconfiguration of protein conformation in a micro and nano particle (MNP) protein corona due to interaction is an often-overlooked aspect in drug design and nano-medicine. Mostly, MNP-Protein corona studies focus on the toxicity of nano particles (NPs) in a biological environment to analyze biocompatibility. However, preserving functional specificity of proteins in an NP corona becomes critical for effective translation of nano-medicine. This paper investigates the non-classical interaction between insulin and ZnO MNPs using a classical electrical characterization technique at GHz frequency with an objective to understand the effect of the micro particle (MP) and nanoparticle (NP) morphology on the electrical characteristics of the MNP-Protein corona and therefore the conformation and functional specificity of protein. The MNP-Protein corona was subjected to thermal and enzymatic (papain) perturbation to study the denaturation of the protein. Experimental results demonstrate that the morphology of ZnO particles plays an important role in preserving the electrical characteristics of insulin.

SUBMITTER: Singh U

PROVIDER: S-EPMC8342705 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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Role of structural specificity of ZnO particles in preserving functionality of proteins in their corona.

Singh Urvashi U Saifi Zeeshan Z Kumar Mridul M Reimers Armin A Krishnananda Soami Daya SD Adelung Rainer R Baum Martina M

Scientific reports 20210805 1

Reconfiguration of protein conformation in a micro and nano particle (MNP) protein corona due to interaction is an often-overlooked aspect in drug design and nano-medicine. Mostly, MNP-Protein corona studies focus on the toxicity of nano particles (NPs) in a biological environment to analyze biocompatibility. However, preserving functional specificity of proteins in an NP corona becomes critical for effective translation of nano-medicine. This paper investigates the non-classical interaction bet ...[more]

PMID: 34354203

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Project description:IntroductionNodulin-26-like intrinsic proteins (NIPs) are integral membrane proteins belonging to the aquaporin family, that facilitate the transport of neutral solutes across the bilayer. The OsNIP2;1 a member of NIP-III class of aquaporins is permeable to beneficial elements like silicon and hazardous arsenic. However, the atomistic cross-talk of these molecules traversing the OsNIP2;1 channel is not well understood.ObjectiveDue to the lack of genomic variation but the availability of high confidence crystal structure, this study aims to highlight structural determinants of metalloid permeation through OsNIP2;1.MethodsThe molecular simulations, combined with site-directed mutagenesis were used to probe the role of specific residues in the metalloid transport activity of OsNIP2;1.ResultsWe drew energetic landscape of OsNIP2;1, for silicic and arsenous acid transport. Potential Mean Force (PMF) construction illuminate three prominent energetic barriers for metalloid passage through the pore. One corresponds to the extracellular molecular entry in the channel, the second located on ar/R filter, and the third size constriction in the cytoplasmic half. Comparative PMF for silicic acid and arsenous acid elucidate a higher barrier for silicic acid at the cytoplasmic constrict resulting in longer residence time for silicon. Furthermore, our simulation studies explained the importance of conserved residues in loop-C and loop-D with a direct effect on pore dynamics and metalloid transport. Next we assessed contribution of predicted key residues for arsenic uptake, by functional complementation in yeast. With the aim of reducing arsenic uptake while maintaining beneficial elements uptake, we identified novel OsNIP2;1 mutants with substantial reduction in arsenic uptake in yeast.ConclusionWe provide a comprehensive assessment of pore lining residues of OsNIP2;1 with respect to metalloid uptake. The findings will expand mechanistic understanding of aquaporin's metalloid selectivity and facilitate variant interpretation to develop novel alleles with preference for beneficial metalloid species and reducing hazardous ones.

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Role of structural specificity of ZnO particles in preserving functionality of proteins in their corona.

Publications

Role of structural specificity of ZnO particles in preserving functionality of proteins in their corona.

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