Volume 12, Issue 47 (7-2022)
NCMBJ 2022, 12(47): 99-114 |
Back to browse issues page
Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
Zakernezhad F, Rasekh B, Maghami P, Yazdian F. Comparison of the effects of functionalized MNPs by mesoporous silica and L-lysine (NH2-Si@Fe3O4) on structural changes of egg white lysozyme protein (HEWL). NCMBJ 2022; 12 (47) :99-114
URL: http://ncmbjpiau.ir/article-1-1479-en.html
URL: http://ncmbjpiau.ir/article-1-1479-en.html
Department of Life Science Engineering, Faculty of New Sciences and Technologies, University of Tehran, Tehran, Iran
Abstract: (2175 Views)
Aim and Background: Adsorption of protein on inorganic surfaces leads to structural and functional changes that depend on the nature of the adsorbed protein and the physicochemical properties of inorganic surfaces. Magnetic nanoparticles (MNPs) with biocompatible coatings are the only FDA-approved nanostructured materials with various applications in medical sciences and unique properties have become a high potential material. Study of the bioimmunity of MNPs requires detailed knowledge of the interaction of MNPs with biological molecules, especially proteins. The present study, Comparison of the effects of functionalized MNPs by mesoporous silica and L-lysine (NH2-Si@Fe3O4) on structural changes of egg white lysozyme protein (HEWL).
Material and Methods: Structural properties and physicochemical characteristics of functionalized MNPs by FTIR, XRD, TEM, FESEM, VSM and DLS analyzes and Protein-nanoparticle interaction was performed using intrinsic fluorescence techniques, ANS test, thioflavin T (ThT) and ATR-FTIR and protein thermal aggregation. Structure change of HEWL on interaction with MNPs was studied.
Conclusion: Investigation of the interaction of HEWL and MNPs with the help of intrinsic fluorescence showed that the binding of proteins to MNPs is influenced by the type of ligand attached to MNPs. Screening thermal aggregation of HEWL in the presence of MNPs revealed the effective role of NH2-Si@Fe3O4 in inhibiting thermal aggregation of HEWL.
Results: Comparison of nanoparticle performance with functional group and without functional group showed that functionalized nanoparticles had better performance; therefore, it is important to consider the environmental, health and safety aspects in the early stages of nanoparticle use. This report provides an integrated picture of protein-MNPs interaction and the change in protein structure after binding to MNPs.
Material and Methods: Structural properties and physicochemical characteristics of functionalized MNPs by FTIR, XRD, TEM, FESEM, VSM and DLS analyzes and Protein-nanoparticle interaction was performed using intrinsic fluorescence techniques, ANS test, thioflavin T (ThT) and ATR-FTIR and protein thermal aggregation. Structure change of HEWL on interaction with MNPs was studied.
Conclusion: Investigation of the interaction of HEWL and MNPs with the help of intrinsic fluorescence showed that the binding of proteins to MNPs is influenced by the type of ligand attached to MNPs. Screening thermal aggregation of HEWL in the presence of MNPs revealed the effective role of NH2-Si@Fe3O4 in inhibiting thermal aggregation of HEWL.
Results: Comparison of nanoparticle performance with functional group and without functional group showed that functionalized nanoparticles had better performance; therefore, it is important to consider the environmental, health and safety aspects in the early stages of nanoparticle use. This report provides an integrated picture of protein-MNPs interaction and the change in protein structure after binding to MNPs.
Type of Study: Research Article |
Subject:
Physiology
Received: 2021/11/16 | Accepted: 2022/01/19 | Published: 2022/04/19
Received: 2021/11/16 | Accepted: 2022/01/19 | Published: 2022/04/19
| Rights and permissions | |
 |
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License. |
