Interaction of acrylamide with proteins in the concentration range used for fluorescence quenching studies

Punyiczki, Mária; Norman, John A. T.; Rosenberg, Andreas

doi:10.1016/0301-4622(93)80028-h

Cited by 21 publications

(16 citation statements)

References 27 publications

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“…In some cases the quenching by penetrating acrylamide molecules can play a dominant role (Somogyi et al, 1994). Furthermore, proteins are able to bind acrylamide (Punyiczki et al, 1993;Matk6 et al, 1980), and the bound acrylamide molecules can also contribute to the quenching. Given the fact that the bimolecular quenching rate constants we found are more than one order of magnitude smaller than those usually obtained for solvent-accessible fluorophores (3-5 X 109 s-1 M-1) (Eftink and Ghiron, 1976) one can conclude that clear interpretation of the acrylamide quenching data requires further study.…”

Section: Mg2tmentioning

confidence: 99%

Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations

Nyitrai¹,

Hild²,

Belágyi³

et al. 1997

Biophysical Journal

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Temperature dependence of the fluorescence intensity and anisotropy decay of N-(iodoacetyl)-N'-(5-sulfo-1-naphthyl)ethylenediamine attached to Cys374 of actin monomer was investigated to characterize conformational differences between Ca- and Mg-G-actin. The fluorescence lifetime is longer in Mg-G-actin than that in Ca-G-actin in the temperature range of 5-34 degrees C. The width of the lifetime distribution is smaller by 30% in Mg-saturated actin monomer at 5 degrees C, and the difference becomes negligible above 30 degrees C. The semiangle of the cone within which the fluorophore can rotate is larger in Ca-G-actin at all temperatures. Electron paramagnetic resonance measurements on maleimide spin-labeled (on Cys374) monomer actin gave evidence that exchange of Ca2+ for Mg2+ induced a rapid decrease in the mobility of the label immediately after the addition of Mg2+. These results suggest that the C-terminal region of the monomer becomes more rigid as a result of the replacement of Ca2+ by Mg2+. The change can be related to the difference between the polymerization abilities of the two forms of G-actin.

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Section: Mg2tmentioning

confidence: 99%

Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations

Nyitrai¹,

Hild²,

Belágyi³

et al. 1997

Biophysical Journal

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“…For BSA only, we see a positive deviation from expected linear relation. This upward curvature is also observed during acrylamide quenching of HSA [44]. The fluorophore (the exposed and buried tryptophan) in such a case is quenched both by collisions (dynamic) and by complex formation (static).…”

Section: Ans Binding To Bsamentioning

confidence: 77%

“…CTAB could be competitively inhibiting the complex formation between acrylamide and BSA. Although in a 300 mM acrylamide solution there are 1000 times molecules present in a 30 mM CTAB solution, the surfactant is able to inhibit the complex formation due to its stronger electrostatic and hydrophobic interaction with BSA compare to weak binding between the acrylamide and the protein molecule [44]. Interestingly the plot has become almost linear on addition of 300 lM CTAB (Fig.…”

Section: Effect Of Surfactants On Acrylamide Quenching Of Bsamentioning

confidence: 93%

Characterization of different conformations of bovine serum albumin and their propensity to aggregate in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide

Sharma

Agarwal

Deep

2010

Journal of Colloid and Interface Science

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“…Molecular oxygen, iodide, bromide ions and acrylamide are common quenchers for almost all dyes [35][36][37][38].…”

Section: Quenching Fluorescencementioning

confidence: 99%

Utilization of Eosin Dye as an Ion Pairing Agent for Determination of Pharmaceuticals: A Brief Review

Rahman

2017

Int J Pharm Pharm Sci

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Globally, dyes are widely used in the pharmaceutical, food, textile, cosmetics, plastics, leather, paint, ink and paper industries. Eosin is an acidic orange-pink dye and has very strong staining properties. Haematoxylin and eosin Y (H and E) combination is the most common staining and primary diagnostic technique in histo-pathological laboratories. This review mainly discussed the utility of eosin dye in quality control laboratories as an ion pairing agent for drug analysis. Eosin Y is one the most common ion pairing agent and its mono and di anionic forms are capable of interacting with many drug molecules to form colored/fluorescent binary or ternary complexes that can be analyzed with or without extraction by spectrofluorimetry and/or spectrophotometry. Quenching fluorescence and advantages of spectrofluorimetry over spectrophotometry were also discussed. Fluorescence detection greatly enhances the sensitivity and providing a sensitive and relatively inexpensive instrumental method of analysis using eosin Y for various important drugs in pure, commercial dosage forms and biological fluids.

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Interaction of acrylamide with proteins in the concentration range used for fluorescence quenching studies

Cited by 21 publications

References 27 publications

Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations

Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations

Characterization of different conformations of bovine serum albumin and their propensity to aggregate in the presence of N-cetyl-N,N,N-trimethyl ammonium bromide

Utilization of Eosin Dye as an Ion Pairing Agent for Determination of Pharmaceuticals: A Brief Review

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