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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.3c01755
|2 doi
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|a pubmed25n1211.xml
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|a (NLM)37878019
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|a DE-627
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Gahtori, Preeti
|e verfasserin
|4 aut
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| 245 |
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|a How Does pH Affect the Adsorption of Human Serum Protein in the Presence of Hydrophobic and Hydrophilic Nanoparticles at Air-Water and Lipid-Water Interfaces?
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|c 2023
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 08.11.2023
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|a Date Revised 18.11.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a This study investigates interaction between hydrophilic (11-mercaptoundecanoic acid (MUA)) and hydrophobic (1-undecanethiol (UDT)) gold nanoparticles (GNPs) with human serum albumin (HSA) protein on air-water and lipid-water interfaces at pH 3 and 7. Vibrational sum frequency generation (VSFG) spectroscopy is used to analyze changes in the intensity of interfacial water molecules and the C-H group of the protein. At the air-water interface, the hydrophobic interaction between the HSA protein and hydrophobic GNPs at pH 3 leads to their accumulation at the interface, resulting in an increased C-H intensity of the protein with a slight decrease in water intensity. Whereas, at pH 7, where the negative charge of the protein results in the reduced surface activity of the HSA compared to pH 3, the interaction between alkyl chain of the hydrophobic GNPs and alkyl group of the protein results in the adsorption of the protein-capped GNPs at the interface. This leads to an increased intensity of the C-H group of protein and water molecules. However, negatively charged hydrophilic GNPs do not induce significant changes in the interfacial water structure or the C-H group of the protein due to the electrostatic force of repulsion with the negatively charged HSA at pH 7. In contrast, at the lipid-water interface, both hydrophobic and hydrophilic GNPs interact with HSA protein, causing disordering of interfacial water molecules at pH 3 and ordering at pH 7. Interestingly, similar behavior of the protein with both types of GNPs results in comparable ordering/disordering at the interface depending on the pH of solution. Furthermore, the VSFG results obtained with the deuterated lipid suggest that changes in ordering and disorder occur due to increased protein adsorption in the presence of GNPs, causing alterations in the membrane structure. These findings give a better understanding of the mechanisms that govern protein-nanoparticle interaction and their consequential effects on the structure, function, and behavior of molecules at the biological membrane interface, which is crucial for developing safe and effective nanoparticle-based therapeutics
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Water
|2 NLM
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|a 059QF0KO0R
|2 NLM
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|a Gold
|2 NLM
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|a 7440-57-5
|2 NLM
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|a Blood Proteins
|2 NLM
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| 650 |
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|a Lipids
|2 NLM
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|a Gunwant, Vineet
|e verfasserin
|4 aut
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| 700 |
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|a Pandey, Ravindra
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 39(2023), 44 vom: 07. Nov., Seite 15487-15498
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnas
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| 773 |
1 |
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|g volume:39
|g year:2023
|g number:44
|g day:07
|g month:11
|g pages:15487-15498
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|u http://dx.doi.org/10.1021/acs.langmuir.3c01755
|3 Volltext
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