Protein G selects two binding sites for carbon nanotube with dissimilar behavior; a molecular dynamics study

Ebrahim-Habibi, Mohammad-Bagher; Ghobeh, Maryam; Mahyari, Farzaneh Aghakhani; Rafii-Tabar, Hashem; Sasanpour, Pezhman

doi:10.1016/j.jmgm.2018.12.007

Cited by 2 publications

(1 citation statement)

References 62 publications

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“…These techniques helped to predict the binding sites of ENPs on proteins, conformational changes of proteins, preference of interaction with different amino acids. ENP-based drug designing for drug delivery is also done using in silico approaches [ 149 , 150 , 151 ]. These studies use online databases available for proteins such as Protein Data Bank (PDB), Swiss-Prot.…”

Section: Techniques To Study Enp-protein Interactionsmentioning

confidence: 99%

Engineered Nanoparticle-Protein Interactions Influence Protein Structural Integrity and Biological Significance

et al. 2022

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Engineered nanoparticles (ENPs) are artificially synthesized particles with unique physicochemical properties. ENPs are being extensively used in several consumer items, elevating the probability of ENP exposure to biological systems. ENPs interact with various biomolecules like lipids, proteins, nucleic acids, where proteins are most susceptible. The ENP-protein interactions are mostly studied for corona formation and its effect on the bio-reactivity of ENPs, however, an in-depth understanding of subsequent interactive effects on proteins, such as alterations in their structure, conformation, free energy, and folding is still required. The present review focuses on ENP-protein interactions and the subsequent effects on protein structure and function followed by the therapeutic potential of ENPs for protein misfolding diseases.

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Section: Techniques To Study Enp-protein Interactionsmentioning

confidence: 99%

Engineered Nanoparticle-Protein Interactions Influence Protein Structural Integrity and Biological Significance

et al. 2022

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<p>Protein–Nanoparticle Interaction: Corona Formation and Conformational Changes in Proteins on Nanoparticles</p>

Park¹

2020

IJN

175

120

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Nanoparticles (NPs) are highly potent tools for the diagnosis of diseases and specific delivery of therapeutic agents. Their development and application are scientifically and industrially important. The engineering of NPs and the modulation of their in vivo behavior have been extensively studied, and significant achievements have been made in the past decades. However, in vivo applications of NPs are often limited by several difficulties, including inflammatory responses and cellular toxicity, unexpected distribution and clearance from the body, and insufficient delivery to a specific target. These unfavorable phenomena may largely be related to the in vivo protein–NP interaction, termed “protein corona.” The layer of adsorbed proteins on the surface of NPs affects the biological behavior of NPs and changes their functionality, occasionally resulting in loss-of-function or gain-of-function. The formation of a protein corona is an intricate process involving complex kinetics and dynamics between the two interacting entities. Structural changes in corona proteins have been reported in many cases after their adsorption on the surfaces of NPs that strongly influence the functions of NPs. Thus, understanding of the conformational changes and unfolding process of proteins is very important to accelerate the biomedical applications of NPs. Here, we describe several protein corona characteristics and specifically focus on the conformational fluctuations in corona proteins induced by NPs.

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Protein G selects two binding sites for carbon nanotube with dissimilar behavior; a molecular dynamics study

Cited by 2 publications

References 62 publications

Engineered Nanoparticle-Protein Interactions Influence Protein Structural Integrity and Biological Significance

Engineered Nanoparticle-Protein Interactions Influence Protein Structural Integrity and Biological Significance

<p>Protein–Nanoparticle Interaction: Corona Formation and Conformational Changes in Proteins on Nanoparticles</p>

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