Quenching of BSA intrinsic fluorescence by alkylpyridinium cations Its relationship to surfactant-protein association

Díaz, X

doi:10.1016/s1010-6030(02)00355-6

Cited by 55 publications

(15 citation statements)

References 14 publications

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“…Much research has been devoted to protein interactions with conventional surfactants such as N , N , N ‐trimethyl‐1‐hexadecanaminium bromide (CTAB), sodium dodecyl sulphate (SDS) and 2‐[4‐(2,4,4‐trimethylpentan‐2‐yl)phenoxy]ethanol (Triton X‐100) but less information is known about Gemini protein surfactant interactions . ‘Gemini surfactant’ is a name given to a family of synthetic amphiphiles possessing, in sequence, a long hydrocarbon chain, an ionic group, a spacer, a second ionic group, and another hydrocarbon tail.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

et al. 2015

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Several spectroscopic approaches namely fluorescence, time-resolved fluorescence, UV-visible, and Fourier transform infra-red (FT-IR) spectroscopy were employed to examine the interaction between ethane-1,2-diyl bis(N,N-dimethyl-N-hexadecylammoniumacetoxy)dichloride (16-E2-16) and bovine serum albumin (BSA). Fluorescence studies revealed that 16-E2-16 quenched the BSA fluorescence through a static quenching mechanism, which was further confirmed by UV-visible and time-resolved fluorescence spectroscopy. In addition, the binding constant and the number of binding sites were also calculated. The thermodynamic parameters at different temperatures (298 K, 303 K, 308 K and 313 K) indicated that 16-E2-16 binding to BSA is entropy driven and that the major driving forces are electrostatic interactions. Decrease of the α-helix from 53.90 to 46.20% with an increase in random structure from 22.56 to 30.61% were also observed by FT-IR. Furthermore, the molecular docking results revealed that 16-E2-16 binds predominantly by electrostatic and hydrophobic forces to some residues in the BSA sub-domains IIA and IIIA.

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Section: Introductionmentioning

confidence: 99%

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

et al. 2015

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“…Interaction of BSA with cationic, anionic and nonionic, and gemini surfactants has been widely studied in the past [24,26,[36][37][38][39][40][41][42][43][44]. However, except a few, most of these studies concerned protein denaturation at surfactant concentrations much above their critical micelle concentration (CMC).…”

Section: Introductionmentioning

confidence: 99%

“…However, at high concentration (>CMC) the protein-surfactant interaction is non-specific in nature and large number of surfactant molecules may attach to a single molecule of protein. Despite numerous reports on binding of FAs and surfactants to BSA [36][37][38][39][40][41][42][43][44], a complete understanding of these interactions is not yet well established. Indeed the structural information on the binding of ligand to BSA is sparse, but indirect evidences of binding of surfactant to HSA suggest that strongly bound surfactant molecules occupy the hydrophobic patches on the surface of the protein molecule [24,29].…”

Section: Introductionmentioning

confidence: 99%

Interaction of bovine serum albumin with N-acyl amino acid based anionic surfactants: Effect of head-group hydrophobicity

Ghosh

Dey

2015

Journal of Colloid and Interface Science

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“…Several N-terminal segments of ACTH were found to have hormonal activities and specific receptor binding properties: ACTH binds to steroidogenic receptors, while ACTH(1-10) was found to bind preferentially to central nervous receptors. The fragment ACTH (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24) is an antagonist for steroidogenesis without any agonist properties [10]. ACTH may enhance memory cytotoxic responses through a combination of mechanisms such as direct cell alterations or synergy with regulatory cytokines [11].…”

Section: Introductionmentioning

confidence: 99%

“…The biomimetic systems were the negatively charged SDS micelles and SDS-PEO aggregates, and the neutral LUTROL® F127 polymeric micelles, in aqueous phosphate buffer solution (PBS). As a tool to obtain information about the location of the Trp residue in the presence of the biomimetic systems, we explored the quenching promoted by alkylpyridinium halides, a family of cationic surfactants containing the pyridinium moiety which is an efficient quencher for tryptophan fluorescence, as verified by the decrease in the fluorescence emission of that residue in BSA and small peptides [22]. The convenience of using alkylpyridinium halides as quencher comes also from their high affinity to amphiphilic aggregates with negatively charged surface like SDS [23] and the dependence of its hydrophobicity on the size of the alkyl chain, whose increase causes reduction of the intramicellar mobility and the exchange rate with the aqueous phase [24].…”

Section: Introductionmentioning

confidence: 99%

Interaction of adrenocorticotropin peptides with microheterogeneous systems — A fluorescence study

Romani¹,

Ito²

2009

Biophysical Chemistry

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Adrenocorticotropin (ACTH) and alpha-melanocyte stimulating hormone (alpha-MSH) are peptides which present many physiological effects related to pigmentation, motor and sexual behavior, learning and memory, analgesia, anti-inflammatory and antipyretic processes. The 13 amino acid residues of alpha-MSH are the same initial sequence of ACTH and due to the presence of a tryptophan residue in position 9 of the peptide chain, fluorescence techniques could be used to investigate the conformational properties of the hormones in different environments and the mechanisms of interaction with biomimetic systems like sodium dodecyl sulphate (SDS) micelles, sodium dodecyl sulphate-poly(ethylene oxide) (SDS-PEO) aggregates and neutral polymeric micelles. In buffer solution, fluorescence parameters were typical of peptides containing tryptophan exposed to the aqueous medium and upon addition of surfactant and polymer molecules, the gradual change of those parameters demonstrated the interaction of the peptides with the microheterogeneous systems. From time-resolved experiments it was shown that the interaction proceeded with conformational changes in both peptides, and further information was obtained from quenching of Trp fluorescence by a family of N-alkylpyridinium ions, which possess affinity to the microheterogeneous systems dependent on the length of the alkyl chain. The quenching of Trp fluorescence was enhanced in the presence of charged micelles, compared to the buffer solution and the accessibility of the fluorophore to the quencher was dependent on the peptide and the alkylpyridinium: in ACTH(1-21) highest collisional constants were obtained using ethylpyridinium as quencher, indicating a location of the residue in the surface of the micelle, while in alpha-MSH the best quencher was hexylpyridinium, indicating insertion of the residue into the non-polar region of the micelles. The results had shown that the interaction between the peptides and the biomimetic systems where driven by combined electrostatic and hydrophobic effects: in ACTH(1-24) the electrostatic interaction between highly positively charged C-terminal and negatively charged surface of micelles and aggregates predominates over hydrophobic interactions involving residues in the central region of the peptide; in alpha-MSH, which presents one residual positive charge, the hydrophobic interactions are relevant to position the Trp residue in the non-polar region of the microheterogeneous systems.

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Quenching of BSA intrinsic fluorescence by alkylpyridinium cations Its relationship to surfactant-protein association

Cited by 55 publications

References 14 publications

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

Spectroscopic and molecular modelling analysis of the interaction between ethane‐1,2‐diyl bis(N,N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin

Interaction of bovine serum albumin with N-acyl amino acid based anionic surfactants: Effect of head-group hydrophobicity

Interaction of adrenocorticotropin peptides with microheterogeneous systems — A fluorescence study

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