Study on the Interaction of Cationic Lipids with Bovine Serum Albumin

Charbonneau, David M.; Tajmir-Riahi, H.A.

doi:10.1021/jp910077h

Cited by 209 publications

(132 citation statements)

References 30 publications

(65 reference statements)

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“…The binding of biomacromolecules to nanoparticles such as GNRs might involve the formation of weak noncovalent forces including hydrogen bonds, van der Waals forces, electrostatic forces, and hydrophobic interaction forces 33. Elucidating the thermodynamic parameters might help provide clues on the involvement of these forces in the conjugation process.…”

Section: Resultsmentioning

confidence: 99%

Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes

et al. 2017

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Gold nanorods (GNRs) are a unique class of metal nanostructures that have attractive potentials in biomedical applications, and the concern on their biological safety is concomitantly increasing. Hemocompatibility is extremely important as their contact with blood circulation is unavoidable during in vivo delivery. Herein, two kinds of GNRs coated with hexadecyltrimethylammonium bromide (C‐GNRs) or poly(sodium‐p‐styrenesulfonate) are used to test their potential toxicological effects in blood. C‐GNRs with positive surface charges efficiently induce hemolysis when encountering erythrocytes. Cellular internalization of C‐GNRs is found, and they subsequently bind with hemoglobin, forming bioconjugates. The interaction between hemoglobin and C‐GNR (stoichiometry 32.7:1) is regulated by electrostatic forces. Chromophores like tryptophan (Trp) are found to interact with C‐GNRs, causing enhancement in fluorescence intensity. The conformation of protein is partially altered, evidenced by decrease in α‐helical, increase in β‐sheet and random coil of hemoglobin. Although C‐GNRs do not essentially decrease oxygen binding capacity of hemoglobin, they hamper oxygen release from the protein. Heme, the oxygen binding unit, releases from hemoglobin upon C‐GNR treatment, which could contribute to C‐GNR‐induced hemolysis. This study demonstrates the hematological effects of GNRs, revealing their potential risk in biomedical applications.

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Section: Resultsmentioning

confidence: 99%

Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes

et al. 2017

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“…Finally, with use of the Gaussian/Lorentzian profile, each spectrum was deconvoluted into seven peaks in the 1700-1600 cm 1 region (Figure 4). According to other protein-related research, the bands can be roughly assigned as follows [42][43][44][45][46][47] antiparallel  sheet increased from 4.2% to 11.1%. The reduction in the  -helix content in favor of the  -sheet, random coil,  -antiparallel and intermolecular  -strand structure is indicative of a partial unfolding of protein in the presence of the AuNPs.…”

Section: 1mentioning

confidence: 96%

Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

Shi

Xie

et al. 2012

Chin. Sci. Bull.

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The interactions between bovine serum albumin (BSA) and gold nanoparticles (AuNPs), and the conformational changes of BSA induced by this interaction, were investigated by UV-visible absorption spectroscopy, fluorescence spectroscopy, and Fourier transform infrared in combination with attenuated total reflection spectroscopy (ATR-FTIR). The critical adsorption density for preventing AuNP aggregation in 0.1 mol/L phosphate buffered saline (pH 7.2) was 23 BSA molecules per gold particle or 3.8×1012 BSA molecules/cm 2 . BSA bound to the AuNPs with high affinity (binding constant K s =7.59×10 8 L/mol), and the intrinsic fluorescence of BSA was quenched by the AuNPs in accordance with the static quenching mechanism. Both fluorescence spectroscopy and ATR-FTIR showed that AuNPs induced conformational changes in BSA, which resulted in it becoming less compact and increased the polarity of the microenvironment around the tryptophan residue Trp-212.

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“…More importantly, BSA is a more hydrophobic protein with high surface activity compared to the highly soluble and charged lysozyme and cytochrome C, and should serve as a better model for membrane proteins. The physicochemical properties of these model proteins are summarized in Table 2 [34,[36][37][38]. The presence of CPEs and OPEs did not induce any changes in the CD spectra of lysozyme or cytochrome C (data not shown), indicating that no conformational changes to the native protein structures were induced.…”

Section: µG Imagementioning

confidence: 98%

“…Lysozyme and cytochrome C are well-folded small globular proteins that have been extensively studied. BSA possesses a high degree of homology with human serum albumin (HAS) [33,34]. Serum albumins are abundant in the mammalian circulatory system and carry out various important physiological functions [35].…”

Section: µG Imagementioning

confidence: 99%

Dark Antimicrobial Mechanisms of Cationic Phenylene Ethynylene Polymers and Oligomers against Escherichia coli

et al. 2011

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Abstract:The interactions of poly(phenylene ethynylene) (PPE)-based cationic conjugated polyelectrolytes (CPEs) and oligo-phenylene ethynylenes (OPEs) with E. coli cells are investigated to gain insights into the differences in the dark killing mechanisms between CPEs and OPEs. A laboratory strain of E. coli with antibiotic resistance is included in this work to study the influence of antibiotic resistance on the antimicrobial activity of the CPEs and OPEs. In agreement with our previous findings, these compounds can efficiently perturb the bacterial cell wall and cytoplasmic membrane, resulting in bacterial cell death. Electron microscopy imaging and cytoplasmic membrane permeability assays reveal that the oligomeric OPEs penetrate the bacterial outer membrane and interact efficiently with the bacterial cytoplasmic membrane. In contrast, the polymeric CPEs cause serious damage to the cell surface. In addition, the minimum inhibitory concentration (MIC) and hemolytic concentration (HC) of the CPEs and OPEs are also measured to compare their antimicrobial activities against two different strains of E. coli with the compounds' toxicity levels against human red blood cells (RBC). MIC and HC measurements are in good agreement with our OPEN ACCESSPolymers 2011, 3 1200 previous model membrane perturbation study, which reveals that the different membrane perturbation abilities of the CPEs and OPEs are in part responsible for their selectivity towards bacteria compared to mammalian cells. Our study gives insight to several structural features of the PPE-based CPEs and OPEs that modulate their antimicrobial properties and that these features can serve as a basis for further tuning their structures to optimize antimicrobial properties.

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Study on the Interaction of Cationic Lipids with Bovine Serum Albumin

Cited by 209 publications

References 30 publications

Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes

Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes

Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin

Dark Antimicrobial Mechanisms of Cationic Phenylene Ethynylene Polymers and Oligomers against Escherichia coli

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