2016
DOI: 10.1039/c6ra16422f
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Thermodynamic and conformational changes of protein toward interaction with nanoparticles: a spectroscopic overview

Abstract: Nanoparticles (NPs) in different forms have been widely used in medicine and pharmaceutics for diagnosis and drug delivery.

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Cited by 94 publications
(44 citation statements)
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“…ΔH°.0 and ΔS°.0 exhibit hydrophobic interactions, ΔH°,0 and ΔS°,0 show hydrogen bonds and van der Waals interactions, and ΔH°,0 and ΔS°.0 represent electrostatic interactions. 40 Negative values of ΔH° (−53.21 kJ/mol) and ΔS° (−42.44 kJ/mol) showed that the NP-induced conformational changes of protein is induced by an enthalpy-driven manner. 40 Likewise, ΔH°,0 and ΔS°,0 are characteristics of hydrogen bonds and van der Waals interactions in aqueous solution.…”
Section: H Rt S Rmentioning
confidence: 96%
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“…ΔH°.0 and ΔS°.0 exhibit hydrophobic interactions, ΔH°,0 and ΔS°,0 show hydrogen bonds and van der Waals interactions, and ΔH°,0 and ΔS°.0 represent electrostatic interactions. 40 Negative values of ΔH° (−53.21 kJ/mol) and ΔS° (−42.44 kJ/mol) showed that the NP-induced conformational changes of protein is induced by an enthalpy-driven manner. 40 Likewise, ΔH°,0 and ΔS°,0 are characteristics of hydrogen bonds and van der Waals interactions in aqueous solution.…”
Section: H Rt S Rmentioning
confidence: 96%
“…40 Negative values of ΔH° (−53.21 kJ/mol) and ΔS° (−42.44 kJ/mol) showed that the NP-induced conformational changes of protein is induced by an enthalpy-driven manner. 40 Likewise, ΔH°,0 and ΔS°,0 are characteristics of hydrogen bonds and van der Waals interactions in aqueous solution. Due to the large surface-to-volume-ratio of NPs, water molecules are substantially adsorbed on their surface and can mediate the establishment of hydrogen bonds between NP and protein.…”
Section: H Rt S Rmentioning
confidence: 96%
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“…Therefore, it is essential to investigate the type of particular interaction in InP/ZnS@BSA conjugates. Hence, thermodynamic parameters are calculated from van't Hoff plots at temperatures 288, 298, 308 and 318 K (see Figure S4a–d). The enthalpy change (Δ H ), entropy change (Δ S ) and Gibbs free energy change (Δ G ) of InP/ZnS@BSA conjugation process are obtained from Equations () and () and results are tabulated in Table .…”
Section: Resultsmentioning
confidence: 99%
“…Surface functionalization of NPs can also influence the protein adsorption and subsequent NP-induced conformational changes. Protein surface residues form an interaction with energetically favorite counterparts on the NP surface based on their charge, hydrophobicity, and hydrophilicity [86].…”
Section: The Effect Of Np On the Protein Conformational Changesmentioning
confidence: 99%