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. anerkjenner støtte fra Duke spesiell initiativ kapitalfond, Wells Fargo fondet, PhRMA Foundation, samt oppstart midler fra University of North Carolina, Charlotte.

1. syntese av BSA-Au(III) kompleks
<ol><li>Oppløse 25 mg BSA i 1 mL av høy ytelse flytende kromatografi (HPLC) klasse vann i 5 mL reaksjon ampuller. Merk: Løsningen skal vises tydelig.</li>
	<li>Oppløse gull (III) klorid trihydrate (chloroauric acid) til en konsentrasjon av 5 mM i HPLC klasse vann. Merk: Løsningen skal vises gule. Chloroauric sur løsning forberedt på denne konsentrasjonen vil resultere i en BSA Au forholdet 1:13.<ol>
<li>Alternativt forberede en løsning av chloroauric syre med en konsentr...

<ol>
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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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BSA-Au(III) forbindelser forberedt ved pH 12 viser rød fluorescens på et utslipp bølgelengde av λem= 640 nm når opphisset med ultrafiolett (UV) lys λex= 365 nm (figur 1A). Fremveksten av røde fluorescens er en langsom prosess og vil ta noen dager ved romtemperatur å øke til en maksimal intensitet. Kjører reaksjonen på 37 ° C vil gi optimale resultater, selv om høyere temperatur kan brukes til å produsere den røde fluorescensen raskere. Uhelbredel...

En BSA-Au sammensatt viser en ultrafiolett (UV)-nervøs røde fluorescens, med bemerkelsesverdig stokes SKIFT, har blitt opprinnelig syntetisert av Xie et al. 1. den unike og stabil røde fluorescensen finner forskjellige programmer i felt som sensing2,3,4, tenkelig5,6,7eller nanomedicine8 ,,9,,10,,11,,12,,13. Denne forbindelsen har vært studert av mange forskere innen nano-vitenskap i årene14,15,16. BSA-Au sammensatte har blitt tolket som Au25 nanoclusters. Målet med presentert metoden er å undersøke denne forbindelsen i detalj og forstå opprinnelsen til den røde fluorescensen. Ved å følge presentert tilnærming, kan tilstedeværelse av flere Au bindende områder, og opprinnelsen til fluorescens, alternativ til ett område nucleation av Au25 nanoclusters, illustreres. Samme tilnærming kan brukes til å studere hvordan andre proteiner17,18,19 kompleksbundet med Au(III) kan endre deres iboende fluorescerende egenskaper.
Syntese av rød-fluorescerende BSA-Au sammensatte krever en smal kontroll av molar prosenter av BSA til Au (BSA:Au) å maksimere intensiteten av fluorescensen og plasseringen av toppene i eksitasjon-utslipp kart (EEM)20. Det kan vises at det finnes flere bindende områder for Au(III) å binde, inkludert Asparagine fragment (eller Asp fragment, fire første aminosyre rester på N-terminus av BSA)21,22. 34th aminosyren av BSA (Cys-34) vises også å koordinere Au(III) og å være involvert i de røde fluorescence([Cys34-capped-BSA]-Au(III))20mekanisme. Cleaving alle Cys-Cys disulfide obligasjoner og capping alle thiols, rød fluorescens er ikke produsert ([all-thiol-capped-BSA]-Au(III)). Dette angir nødvendigheten av Cys-Cys disulfide obligasjoner som Au(III) binding til å produsere den røde fluorescensen.
Protein kjemi teknikker har ikke vært mye brukt til å studere BSA-Au(III) komplekser i nano-forskningsmiljøet. Men ville det være verdifullt å bruke disse teknikkene til å forstå enkelte aspekter av disse kompleksene, så vel som å få detaljert forståelse av de Au(III) binding i BSA. Denne artikkelen er ment å vise noen av disse teknikkene.

<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 presentert protokollene er å studere prosessen med Au(III) binding til BSA, gir konformasjon forårsaket røde fluorescens (λem = 640 nm) av BSA-Au(III) komplekser. Metoden som justerer pH for å vise at fremveksten av den røde fluorescensen er korrelert med pH-indusert likevekt overganger av BSA konformasjonen. Rød fluorescerende BSA-Au(III) komplekser kan bare utformes med en tilpasning av pH på eller over 9,7, som tilsvarer "Et-skjema" konformasjon av BSA. Protokollen å justere BSA Au molar forhold og overvåke tid-løpet av prosessen med Au(III) binding er beskrevet. Minste antall Au(III) per BSA, å produsere den røde fluorescensen, er mindre enn sju. Vi beskriver protokollen i trinn for å illustrere tilstedeværelsen av flere Au(III) bindende områder i BSA. Først, ved å legge kobber (Cu(II)) eller nikkel (Ni(II)) kasjoner etterfulgt av Au(III), denne metoden viser en binding området for Au(III) som ikke er den røde fluorophore. Andre, ved å endre BSA av thiol capping agenter, en annen nonfluorophore-forming Au(III) binding området er avslørt. Tredje illustrert endre BSA konformasjon av cleaving og capping av disulfide obligasjoner, mulig Au(III) binding område(r). Protokollen beskrevet, for å kontrollere BSA konformasjonen og Au(III)-tilknytning kan brukes generelt for å studere samspillet av andre proteiner og metall kasjoner.

Fra fluorescens av BSA-Au(III) komplekset, det har blitt observert at konvertering av den iboende blå fluorescensen av BSA (λem = 400 nm) til rød fluorescens (λem = 640 nm) omtrent pH 9,7 gjennom en likevekt Overgang (figur 1). EEM av BSA-Au(III) på ulike BSA til Au molar prosenter er vist i figur 2, og disse dataene viser hvordan endre molar forholdstallene gir samme utslipp bølgelen...

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

Protokollene for studerer binding av gull kasjoner (Au(III)) til ulike konformasjonen av bovin serum albumin (BSA) så vel som karakteriserer den conformational avhengige unike BSA-Au fluorescensen presenteres.

Luminophore formasjon i ulike konformasjonen av bovin Serum Albumin ved Binding av 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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