The Complex of Apomyoglobin with the Fluorescent Dye Coumarin 153¶

Chowdhury, P. K.; Halder, Mintu; Sanders, L.; Arnold, R. A.; Liu, Y.; Armstrong, Daniel W.; Kundu, Suman; Hargrove, Mark S.; Song, Xueyu; Petrich, Jacob W.

doi:10.1562/ra-020r.1

Cited by 20 publications

(31 citation statements)

References 60 publications

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“…While DANCA and ANSDMA are both capable of charge transfer in the excited state, coumarin 153 is exquisitely inert, which is one of the reasons it has been so extensively employed as a probe of solvation. 57,[62][63][64][65][66][67][68][69][70][71][72][73] (The DANCA experiments used an excitation wavelength of 345 nm. Novaira et al have observed that both LE and CT emission can be observed in reverse micelles at 330 nm.…”

Section: L(t) )mentioning

confidence: 99%

Solvation Dynamics of the Fluorescent Probe PRODAN in Heterogeneous Environments: Contributions from the Locally Excited and Charge-Transferred States

2009

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The coexistence of different excited states with different properties of the same chromophores could have significant consequences for the accurate characterization of solvation dynamics in a heterogeneous environment, such as a protein. The purpose of this work is to study the contributions of the locally excited (LE) and charge-transferred (CT) states of the fluorescent probe molecule 6-propionyl-2-(N,Ndimethylamino)naphthalene (PRODAN) to its solvation dynamics in the heterogeneous environment provided by reverse micelles formed by sodium 1,4-bis-(2-ethylhexyl) sulfosuccinate (AOT)/n-heptane/ water. We have found that the LE and CT states of PRODAN solvate on different time scales in reverse micelles (2 and ∼0.4 ns, respectively), consistent with results suggested in the literature, and have concluded that PRODAN's use as a probe of heterogeneous environments must be used with caution and that, more importantly, the same caution must be exercised with any chromophore capable of emitting from different excited states. ReceiVed: June 1, 2009; ReVised Manuscript ReceiVed: July 20, 2009 The coexistence of different excited states with different properties of the same chromophores could have significant consequences for the accurate characterization of solvation dynamics in a heterogeneous environment, such as a protein. The purpose of this work is to study the contributions of the locally excited (LE) and charge-transferred (CT) states of the fluorescent probe molecule 6-propionyl-2-(N,N-dimethylamino)naphthalene (PRODAN) to its solvation dynamics in the heterogeneous environment provided by reverse micelles formed by sodium 1,4-bis-(2-ethylhexyl) sulfosuccinate (AOT)/n-heptane/water. We have found that the LE and CT states of PRODAN solvate on different time scales in reverse micelles (2 and ∼0.4 ns, respectively), consistent with results suggested in the literature, and have concluded that PRODAN's use as a probe of heterogeneous environments must be used with caution and that, more importantly, the same caution must be exercised with any chromophore capable of emitting from different excited states.

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Section: L(t) )mentioning

confidence: 99%

Solvation Dynamics of the Fluorescent Probe PRODAN in Heterogeneous Environments: Contributions from the Locally Excited and Charge-Transferred States

2009

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“…As mentioned above, some species of coumarin derivative interact with myoglobin, according to the literature reported previously [25]. On these grounds, we investigated myoglobin recognition abilities of 1a and 1b by fluorescence spectroscopy.…”

Section: Guest-binding Behavior Of Coumarin-appended Cyclophanesmentioning

confidence: 70%

“…Among them, coumarin and its derivatives take advantages in a viewpoint of their high quantum yield, thermal stability, and less toxicity [24]. In particular, a certain coumarin derivative was known to exhibit binding affinity toward myoglobin [25]. In the series of our research on fluorophore-appended cyclophanes, we began to develop coumarin-appended cyclophanes with the aim of sensing for specific proteins.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of coumarin-appended cyclophanes and evaluation of their complexation with myoglobin

Hayashida

Harada

Kojima

2015

J Incl Phenom Macrocycl Chem

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Coumarin-appended cyclophanes bearing positively or negatively charged side chains were synthesized as a water-soluble host (1a or 1b, respectively). Host 1a and 1b showed fluorescence bands with fluorescence maxima at 404 nm originated from coumarin moiety. As a host for guest molecules by using macrocyclic cavity, cationic host 1a binds anionic guests such as 6-p-toluidinonaphthalene-2-sulfonate (TNS), 6-anilinonaphthalene-2-sulfonate (2,6-ANS), and 8-anilinonaphthalene-1-sulfonate (1,8-ANS) more strongly than anionic host 1b, reflecting intermolecular electrostatic interactions. In addition, both host 1a and 1b showed protein surface recognition and fluorescence response toward myoglobin, a small and globular protein. The fluorescence intensity originating from the hosts decreased upon the addition of myoglobin, reflecting the formation of 1a-and 1b-myoglobin complexes. On the other hand, such fluorescence response of 1a and 1b was almost negligible for other proteins such as egg white albumin, bovine serum albumin, human albumin, concanavaline A, fibrinogen, c-globlin, peanut agglutinin, trypsin, and lysozyme.

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“…CZE was used to study b-amyloid and its aggregation [275], botulinum neurotoxin B light chain activity [276], nonenzymatic posttranslation modifications on BSA [277], aminoacyl-tRNA synthetase localized in cell nucleus [278], protein-protein interactions [279], aggregation and denaturation of antibodies [280], glycosylation of murine erythropoietin [281], PEGylation of proteins [282], glutamine deamidation in proteins [283], complexation of apomyoglobin with Coumarin 153 [284], reaction of FQ with ovalbumin [285], interaction of GFP with calcium [286], noncovalent complexation in myoglobin [287], DNA-protein interactions [288][289][290], binding fucoidan to antithrombin [291], retinoic acid to b-lactoglobulin B [292], and binding phospholipid and glycosaminoglycan to human b 2 -glycoprotein [293].…”

Section: Other Proteinsmentioning

confidence: 99%

Capillary electrophoresis of proteins 2003–2005

Dolnı́k¹

2006

Electrophoresis

139

117

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This review article with 304 references describes recent developments in CE of proteins, and covers the two years since the previous review (Hutterer, K., Dolník, V., Electrophoresis 2003, 24, 3998-4012) through Spring 2005. It covers topics related to CE of proteins, including modeling of the electrophoretic migration of proteins, sample pretreatment, wall coatings, improving separation, various forms of detection, special electrophoretic techniques such as affinity CE, CIEF, and applications of CE to the analysis of proteins in real-world samples including human body fluids, food and agricultural samples, protein pharmaceuticals, and recombinant protein preparations.

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The Complex of Apomyoglobin with the Fluorescent Dye Coumarin 153¶

Cited by 20 publications

References 60 publications

Solvation Dynamics of the Fluorescent Probe PRODAN in Heterogeneous Environments: Contributions from the Locally Excited and Charge-Transferred States

Solvation Dynamics of the Fluorescent Probe PRODAN in Heterogeneous Environments: Contributions from the Locally Excited and Charge-Transferred States

Synthesis of coumarin-appended cyclophanes and evaluation of their complexation with myoglobin

Capillary electrophoresis of proteins 2003–2005

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