Name: luminophore formation in various conformations of bovine serum albumin by binding of gold(iii)
Uploaded: 2018-08-31T15:00:00
Description: Watch this Scientific Journal Video about Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII at JoVE.com

S.E. anerkender støtte fra hertug Endowment særlige initiativ Fund, Wells Fargo Fund, PhRMA Foundation samt start midler fra University of North Carolina, Charlotte.

1. Sammenfatning af BSA-Au(III) kompleks
<ol><li>25 mg BSA i 1 mL af high-performance væskekromatografi (HPLC) vand i en 5 mL prøveglas opløses. Bemærk: Løsningen bør vises klart.</li>
	<li>Opløse guld (III) chlorid trihydrat (chloroauric syre) til en koncentration på 5 mM i vand af HPLC-renhed. Bemærk: Løsningen bør vises gule. Chloroauric syre opløsning fremstillet ved denne koncentration vil resultere i en BSA Au forhold på 1:13.<ol>
<li>Alternativt kan du forberede en opløsning af chloroauric sy...

<ol>
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M., Egusa, S. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Conformational+Change-Induced+Fluorescence+of+Bovine+Serum+Albumin-Gold+Complexes.">Conformational Change-Induced Fluorescence of Bovine Serum Albumin-Gold Complexes.</a> Journal of the American Chemical Society. 140, 2265-2271 (2018).</li><li>Peters, T. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=.">.</a> All About Albumin. , (1996).</li><li>Masuoka, J., Saltman, P. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Zinc(II)+and+Copper(II)+Binding+to+Serum+Albumin.+A+Comparative+Study+of+Dog,+Bovine,+and+Human+Albumin.">Zinc(II) and Copper(II) Binding to Serum Albumin. A Comparative Study of Dog, Bovine, and Human Albumin.</a> Journal of Biological Chemistry. 269, 25557-25561 (1994).</li><li>Takeda, K., Wada, A., Yamamoto, K., Moriyama, Y., Aoki, K. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Conformational+Change+of+Bovine+Serum+Albumin+by+Heat+Treatment.">Conformational Change of Bovine Serum Albumin by Heat Treatment.</a> Journal of Protein Chemistry. 8 (5), 653-659 (1989).</li><li>Klotz, I. M., Curme, H. G. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=The+Thermodynamics+of+Metallo-protein+Combinations.+Copper+with+Bovine+Serum+Albumin.">The Thermodynamics of Metallo-protein Combinations. Copper with Bovine Serum Albumin.</a> Journal of the American Chemical Society. 70, 939-943 (1948).</li><li>Fiess, H. A., Klotz, I. 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De BSA-Au(III) forbindelser forberedt på pH 12 udviser rød fluorescens ved en emission bølgelængde på λem= 640 nm når ophidset med ultraviolet (UV) lys λex= 365 nm (figur 1A). Fremkomsten af røde Fluorescens er en langsom proces, og vil tage et par dage ved stuetemperatur til at stige til en maksimal intensitet. Kører reaktionen ved 37 ° C vil give optimale resultater, selvom højere temperatur kan bruges til at producere den røde fluorescens hurtig...

En BSA-Au sammensatte udstiller en ultraviolet (UV)-overgearet røde fluorescens, med bemærkelsesværdig stokes Skift, har været oprindeligt syntetiseret af Xie mfl. 1. den unikke og stabil rød fluorescens kan finde forskellige applikationer på områder som sensing2,3,4, imaging5,6,7, eller Nanomedicin8 ,9,10,11,12,13. Dette stof er blevet undersøgt udførligt af mange forskere inden for nano-videnskaben i de senere år14,15,16. BSA-Au sammensatte er blevet fortolket som Au25 nanoclusters. Målet med den præsenterede metode er at undersøge dette stof i detaljer og forstå oprindelsen af den røde fluorescens. Ved at følge den præsenterede tilgang, kan tilstedeværelsen af flere Au bindingssteder, og oprindelsen af fluorescens, alternativ til single-site Nukleering af Au25 nanoclusters, illustreres. Den samme fremgangsmåde kan anvendes til at studere hvordan andre proteiner17,18,19 kompleksbundet med Au(III) kan ændre deres iboende fluorescerende egenskaber.
Syntese af rødt-fluorescerende BSA-Au stof kræver en smal kontrol af de molære forhold for BSA til Au (BSA:Au) at maksimere intensiteten af fluorescens og placeringen af toppene i excitation-emission kort (EEM)20. Det kan påvises, at flere bindingssteder findes for Au(III) at binde, herunder asparagin fragment (eller Asp fragment, de første fire aminosyrerester på N-terminus af BSA)21,22. 34th aminosyren af BSA (Cys-34) er også vist at koordinere Au(III) og inddrages i mekanismen af rød fluorescence([Cys34-capped-BSA]-Au(III))20. Når alle Cys-Cys disulfid obligationer og loft over alle dithioler, røde Fluorescens er ikke produceret ([all-thiol-capped-BSA]-Au(III)). Dette viser nødvendigheden af Cys-Cys disulfid obligationer som Au(III) bindingssted til at producere den røde fluorescens.
Protein kemi teknikker har ikke været udbredt at studere BSA-Au(III) komplekser i Fællesskabets nano-science. Det ville imidlertid være værdifulde at anvende disse teknikker til at forstå visse aspekter af disse komplekser, samt at opnå detaljeret forståelse af Au(III) bindingsstederne i BSA. Denne artikel er bestemt til at vise nogle af disse teknikker.

<table>
	<tbody>
		<tr>
			<td>Bovine Serum Albumin (BSA), 96%</td>
			<td>Sigma-Aldrich</td>
			<td>A5611</td>
			<td></td>
		</tr>
		<tr>
			<td>gold (III) chloride trihydrate, 99.9%</td>
			<td>Sigma-Aldrich</td>
			<td>520918</td>
			<td></td>
		</tr>
		<tr>
			<td>Copper (II) chloride dihydrate, 99.999%</td>
			<td>Sigma-Aldrich</td>
			<td>459097</td>
			<td></td>
		</tr>
		<tr>
			<td>Nickel (II) chloride hexahydrate, 99.9%</td>
			<td>Sigma-Aldrich</td>
			<td>654507</td>
			<td></td>
		</tr>
		<tr>
			<td>N-Ethylmaleimide (NEM), &#62;99.0%</td>
			<td>Sigma-Aldrich</td>
			<td>4259</td>
			<td></td>
		</tr>
		<tr>
			<td>Tris(2-carboxyethyl)phosphine hydrochloride (TCEP), &#62;98.0%</td>
			<td>Sigma-Aldrich</td>
			<td>C4706</td>
			<td></td>
		</tr>
		<tr>
			<td>Sodium hydroxide, &#62;98.0%</td>
			<td>Sigma-Aldrich</td>
			<td>S8045</td>
			<td></td>
		</tr>
		<tr>
			<td>Urea, 99.5%</td>
			<td>Chem-Implex Int&#39;l</td>
			<td>30142</td>
			<td></td>
		</tr>
		<tr>
			<td>Phospate buffered saline (PBS)</td>
			<td>Corning</td>
			<td>MT21040CV</td>
			<td></td>
		</tr>
		<tr>
			<td>Ammonium bicarbonate, 99.5%</td>
			<td>Sigma-Aldrich</td>
			<td>9830</td>
			<td></td>
		</tr>
	</tbody>
</table>

luminophore formation in various conformations of bovine serum albumin by binding of gold(iii)

Formålet med de præsenterede protokoller er at studere processen med Au(III) binding til BSA, giver kropsbygning ændring-induceret røde fluorescens (λem = 640 nm) af BSA-Au(III) komplekser. Metoden justerer pH for at vise, at fremkomsten af den røde Fluorescens er korreleret med pH-induceret ligevægt overgange af BSA konformationer. Rødt fluorescerende BSA-Au(III) komplekser kan kun dannes med en justering af pH på eller over 9.7, hvilket svarer til "En-formular" kropsbygning af BSA. Protokol til at justere BSA Au molære forhold og overvåge tidsforløb i processen med Au(III) bindende er beskrevet. Det mindste antal Au(III) pr. BSA, til at producere den røde fluorescens, er mindre end syv. Vi beskriver protokol i skridt til at illustrere tilstedeværelsen af flere Au(III) bindingssteder i BSA. Første, ved at tilføje kobber (Cu(II)) eller nikkel (Ni(II)) kationer efterfulgt af Au(III), denne metode afslører en bindingssted for Au(III), der ikke er den røde fluorophore. For det andet ved at ændre BSA af thiol udjævningen agenter, er en anden nonfluorophore-dannende Au(III) bindingssted afsløret. For det tredje er ændrer BSA kropsbygning af holde og udjævningen af disulfid obligationer, muligt Au(III) bindende kvadratnetsreference illustreret. Protokollen beskrevet, for at styre BSA konformationer og Au(III) bindende, kan anvendes generelt til at undersøge interaktioner med andre proteiner og metal kationer.

Fra fluorescens af BSA-Au(III)-komplekset, det er blevet bemærket at omdannelse af den iboende blå fluorescens af BSA (λem = 400 nm) til røde fluorescens (λem = 640 nm) opstår på om pH 9,7 gennem en ligevægt overgang (figur 1). EEM af BSA-Au(III) på forskellige BSA til Au molære forhold er vist i figur 2, og disse data viser, hvordan at ændre de molære forhold giver den samme em...

Watch this Scientific Journal Video about Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII at JoVE.com

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII

Protokoller for at studere bindingen af guld kationer (Au(III)) til forskellige konformationer af bovint serumalbumin (BSA) så godt som kendetegner den konformationelle afhængige unikke BSA-Au fluorescens præsenteres.

Luminophore dannelse i forskellige konformationer af bovint serumalbumin ved Binding af Gold(III)

The purpose of the presented protocols is to study the process of Au(III) binding to BSA, yielding conformation change-induced red fluorescence (&#955;em ...

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Chemistry

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

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