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  1. Article ; Online: Protein-Mediated Changes in Membrane Fluidity and Ordering: Insights into the Molecular Mechanism and Implications for Cellular Function.

    Gunwant, Vineet / Gahtori, Preeti / Varanasi, Srinivasa Rao / Pandey, Ravindra

    The journal of physical chemistry letters

    2024  Volume 15, Issue 16, Page(s) 4408–4415

    Abstract: Probing protein-membrane interactions is vital for understanding biological functionality for various applications such as drug development, targeted drug delivery, and creation of functional biomaterials for medical and industrial purposes. In this ... ...

    Abstract Probing protein-membrane interactions is vital for understanding biological functionality for various applications such as drug development, targeted drug delivery, and creation of functional biomaterials for medical and industrial purposes. In this study, we have investigated interaction of Human Serum Albumin (HSA) with two different lipids, dipalmitoylphosphatidylglycerol (dDPPG) and dipalmitoylphosphatidylcholine (dDPPC), using Vibrational Sum Frequency Generation spectroscopy at different membrane fluidity values. In the liquid-expanded (LE) state of the lipid, HSA (at pH 3.5) deeply intercalated lipid chains through a combination of electrostatic and hydrophobic interactions, which resulted in more ordering of the lipid chains. However, in the liquid-condensed (LC) state, protein intercalation is decreased due to tighter lipid packing. Moreover, our findings revealed distinct differences in HSA's interaction with dDPPG and dDPPC lipids. The interaction with dDPPC remained relatively weak compared to dDPPG. These results shed light on the significance of protein mediated changes in lipid characteristics, which hold considerable implications for understanding membrane protein behavior, lipid-mediated cellular processes, and lipid-based biomaterial design.
    MeSH term(s) Humans ; Phosphatidylglycerols/chemistry ; Phosphatidylglycerols/metabolism ; Membrane Fluidity ; 1,2-Dipalmitoylphosphatidylcholine/chemistry ; Hydrophobic and Hydrophilic Interactions ; Serum Albumin, Human/chemistry ; Serum Albumin, Human/metabolism ; Static Electricity
    Chemical Substances Phosphatidylglycerols ; 1,2-Dipalmitoylphosphatidylcholine (2644-64-6) ; 1,2-dipalmitoylphosphatidylglycerol (VA9U6BR3SB) ; Serum Albumin, Human (ZIF514RVZR)
    Language English
    Publishing date 2024-04-16
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7185
    ISSN (online) 1948-7185
    DOI 10.1021/acs.jpclett.3c03627
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: 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?

    Gahtori, Preeti / Gunwant, Vineet / Pandey, Ravindra

    Langmuir : the ACS journal of surfaces and colloids

    2023  Volume 39, Issue 44, Page(s) 15487–15498

    Abstract: 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. ... ...

    Abstract 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.
    MeSH term(s) Humans ; Water/chemistry ; Adsorption ; Gold/chemistry ; Metal Nanoparticles ; Blood Proteins ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Lipids/chemistry
    Chemical Substances Water (059QF0KO0R) ; Gold (7440-57-5) ; Blood Proteins ; Lipids
    Language English
    Publishing date 2023-10-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/acs.langmuir.3c01755
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Unravelling the Mechanism behind Charge Reversal at Silica Nanoparticle-Model Cell Membrane Interfaces.

    Gahtori, Preeti / Mishra, Akriti / Varanasi, Srinivasa Rao / Pandey, Ravindra

    The journal of physical chemistry. B

    2023  Volume 127, Issue 18, Page(s) 4072–4080

    Abstract: Vibrational sum frequency generation spectroscopy is used to understand the interactions of silica nanoparticles (SNPs) with a model cationic membrane (1,2-dipalmitoyl-3-(trimethylammonium)propane, DPTAP) by monitoring changes in the interfacial water ... ...

    Abstract Vibrational sum frequency generation spectroscopy is used to understand the interactions of silica nanoparticles (SNPs) with a model cationic membrane (1,2-dipalmitoyl-3-(trimethylammonium)propane, DPTAP) by monitoring changes in the interfacial water and lipid structure at pH ∼ 2 and pH ∼ 11. Our study reveals that, at pH ∼ 11, SNPs are attracted to DPTAP due to electrostatic forces, causing changes in the interfacial water structure and lipid membrane. At high concentrations of SNPs (≥70 pM), the interfacial charge reversed from positive to negative, inducing the formation of new hydrogen-bonded structures and reorganization of water molecules. Conversely, negligible changes are observed at pH ∼ 2 due to nearly neutral charge of the SNPs. Molecular dynamics simulations demonstrated that the interfacial potential due to model membrane and SNPs dictates the water structure at the interface. These results elucidate the fundamental mechanism governing interfacial interactions and could have implications in drug delivery, gene therapy, and biosensing.
    MeSH term(s) Silicon Dioxide ; Cell Membrane ; Water/chemistry ; Spectrum Analysis/methods ; Lipids/chemistry
    Chemical Substances Silicon Dioxide (7631-86-9) ; Water (059QF0KO0R) ; Lipids
    Language English
    Publishing date 2023-04-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.3c02402
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Spectral Response of Interfacial Water at Different Lipid Monolayer Interfaces upon Interaction with Charged Gold Nanoparticles

    Gahtori, Preeti / Varanasi, Srinivasa Rao / Pandey, Ravindra

    Journal of physical chemistry. 2021 Sept. 20, v. 125, no. 38

    2021  

    Abstract: Understanding the interactions of nanoparticles with cell membranes is crucial for designing materials for biomedical applications. In this paper, through the combination of vibrational sum frequency generation (VSFG) and molecular dynamics simulation ... ...

    Abstract Understanding the interactions of nanoparticles with cell membranes is crucial for designing materials for biomedical applications. In this paper, through the combination of vibrational sum frequency generation (VSFG) and molecular dynamics simulation techniques, the spectral responses of the interfacial water molecules due to interaction of anionic gold nanoparticles (AGNPs) and cationic gold nanoparticles (CGNPs) with three differently charged model cell membranes, namely, 1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol (DPPG, negatively charged), 1,2-dipalmitoyl-3-trimethylammonium-propane (DPTAP, positively charged), and zwitterionic 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC, neutral), have been investigated. The interfacial water intensity at the DPPG–water interface decreases abruptly in the presence of CGNPs because of the significant change in Stern layer configuration, whereas it does not show any noticeable change in the presence of AGNPs, resulting in an unperturbed stern layer configuration. However, in the case of DPTAP and DPPC interfaces, the Stern layer is significantly perturbed in the presence of both the charged GNPs, resulting in a substantial change in the interfacial water intensity. This is attributed to the change in orientation and structure of interfacial water molecules in the presence of both charged GNPs. These results provide valuable insights into the solvation structure and dynamics of water molecules to exploit for designing and optimizing the delivery system for biomedical applications.
    Keywords lipids ; molecular dynamics ; nanogold ; solvation ; zwitterions
    Language English
    Dates of publication 2021-0920
    Size p. 21234-21245.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1932-7455
    DOI 10.1021/acs.jpcc.1c06556
    Database NAL-Catalogue (AGRICOLA)

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