남동 시작 자금에서 노스 캐롤라이나 대학, 뿐만 아니라 듀크 기부 특별 한 이니셔티브 기금, 웰 스 파고 기금, PhRMA 재단에서 지원 샬 롯을 인정합니다.

1입니다. 복잡 한 BSA-Au(III)의 합성
<ol><li>고성능 액체 크로마토그래피 (HPLC) 학년 물 5 mL 반응 유리병에서의 1 mL에 BSA의 25 mg을 디졸브. 참고: 솔루션 분명 나타납니다.</li>
	<li>HPLC 학년 물에 5 m m의 농도에 금 (III) 염화 물 안내 (chloroauric 산)을 분해. 참고: 솔루션 노란색 나타납니다. Chloroauric 산 성 솔루션이이 농도에서 준비는 BSA Au 비율 1시 13분의 발생 합니다.<ol>
<li>어디의 농도와 chloroauric 산의 솔루션을 준비 또는 0.38 m m 사이 (BSA:Au = 1:1) 20 m m (BSA:Au = 1시 50분) HPLC에 학년 물. 참고: 금 BSA의 다른 비율 여기 방출 지도 크게 다른 빨간 형광 패턴에 발생 합니다.</li>
	</ol>
</li>
	<li>37 ° C 물 욕조에 BSA의 반응 유리병을 배치 하 고 적극적으로 자력을 사용 하 여 750 rpm에서 저 어.</li>
	<li>교 반 시작, 후에 즉시 솔루션에 chloroauric 산의 1 mL를 추가 합니다. 솔루션의 색 노란색 클리어에서 변환 해야 합니다.</li>
	<li>37 ° C에서와 750 rpm는 자력을 사용 하 여 2 분 동안 혼합물을 저 어.</li>
	<li>반응 유리병으로 1 M NaOH의 100 μ 12 pH를가지고 솔루션을 추가 합니다. 참고: NaOH를 추가 후에 즉시 솔루션 노란색-갈색으로 약간 어둡게 한 해야 다음 다시 노란색으로 설정 합니다.</li>
	<li>2 h 750 rpm에서 고 37 ° c.에 저 어로 진행 솔루션 천천히 어두운 노랑/브라운 색상을 노란색에서 변경 해야 합니다. 이 색깔 변화 복잡 한 붉은 fluorescing BSA-Au(III)의 형성을 나타냅니다.</li>
	<li>2 일 동안 실내 온도에 앉아 샘플을 허용 하 고 솔루션 황색 갈색 어둡게 하 계속 되 고 형광 강도 증가.<ol>
<li>또는, 샘플 솔루션의 컬러는 주황색 갈색에 발전 함에 따라 더 많은 h 12 37 ° C에서 저를 계속 하자.</li>
	</ol>
</li>
</ol>2입니다. BSA-Cu(II)-Au(III)의 합성
<ol><li>HPLC 학년 물의 1 mL에서 BSA의 25 mg을 디졸브. 솔루션은 분명 나타납니다.</li>
	<li>HPLC 학년 물 5 m m의 농도에 구리 (II) 염화 물이 수화물을 디졸브. 솔루션 빛 나타납니다 파란색.</li>
	<li>5 mL 반응 유리병을 BSA 용액 1 mL를 추가 하 고 37 ° c.에 물 욕조에 배치 750 rpm에 혼합물을 저 어.</li>
	<li>즉시 반응 유리병에 구리 (II) 염화 물이 수화물 해결책의 0.5 mL을 추가 하 고 2 분에 대 한 믹스. 솔루션 빛 남아 블루.</li>
	<li>하는 pH 12 2 h에 대 한 혼합 수 1 M NaOH의 75 μ를 추가 합니다. 솔루션은 보라색 될 것입니다.</li>
	<li>HPLC 학년 물 5 m m의 농도에 chloroauric 산을 분해.</li>
	<li>반응 유리병에 수성 chloroauric 산의 0.5 mL을 추가 하 고 다시 1 M NaOH를 사용 하 여 12에 pH를 조정.</li>
	<li>2 시간에 대 한 반응 혼합물을 저 어. 참고: 솔루션 갈색 색상으로 진화 한다.</li>
</ol>3입니다. BSA-Ni(II)-Au(III)의 합성
<ol><li>HPLC 학년 물의 1 mL에서 BSA의 25 mg을 디졸브. 솔루션은 분명 나타납니다.</li>
	<li>니켈 (II) 염화 물 hexahydrate 5 m m의 농도를 HPLC 학년 물에 용 해. 솔루션 나타납니다 빛 녹색.</li>
	<li>5 mL 반응 유리병에 BSA 용액 1 mL를 추가 하 고 750 rpm에 혼합물 37 oC. 볶음에 물 욕조에 배치.</li>
	<li>즉시 반응 유리병을 2 분 동안 혼합 니켈 (II) 염화 물 hexahydrate 솔루션의 0.5 mL를 추가 합니다. 참고: 솔루션 빛 유지 됩니다 녹색.</li>
	<li>하는 pH 12 2 h에 대 한 혼합 수 1 M NaOH의 75 μ를 추가 합니다. 참고: 솔루션 어두운 노란색 될 것입니다.</li>
	<li>HPLC 학년 물 5 m m의 농도에 chloroauric 산을 분해.</li>
	<li>반응 유리병에 수성 chloroauric 산의 0.5 mL을 추가 하 고 pH 12 다시 조정 합니다.</li>
	<li>2 시간에 대 한 반응 혼합물을 저 어. 참고: 솔루션 갈색 색상으로 진화 한다.</li>
</ol>4입니다. [Cys34-capped-BSA]-Au(III)의 합성
<ol><li>버퍼링 하는 인산 염 (PBS, pH 7.4)의 1 mL에 N-ethylmaleimide (NEM)의 2 밀리 그램을 디졸브.</li>
	<li>1 mL의 PBS NEM 솔루션에 BSA의 2 밀리 그램을 디졸브.</li>
	<li>5 mL 반응 유리병에 솔루션을 전송 하 고 1 시간에 500 rpm에서 20 ° C에서 저 어.</li>
	<li>500 mL PBS, unreacted NEM 제거를 자력 하룻밤 함께 50 rpm에서 교 반에 12 kDa 투 석 튜브를 사용 하 여 솔루션 dialyze</li>
	<li>0.4 m m의 농도에 PBS에 chloroauric 산을 분해. 참고: 솔루션 희미 한 노란색을 될 것입니다.</li>
	<li>37 ° c.에 물 목욕을 반응 유리병을 전송 750 rpm에서 저 어.</li>
	<li>즉시 반응 유리병에 chloroauric 산 성 해결책의 1 mL을 추가 하 고 2 분 대 혼합을 허용.</li>
	<li>PH 12를가지고 고 2 h에 대 한 혼합 반응 유리병에 1 M NaOH의 75 μ를 추가 합니다.</li>
</ol>5입니다. [all-thiol-capped-BSA]-Au(III)의 합성
<ol><li>2 M 요소와 50 m m 염화 중 탄산염 (NH4HCO3, pH 8.0) HPLC 학년 물에의 한 솔루션을 준비 합니다.</li>
	<li>위의 솔루션의 5 mL 반응 유리병에 1 mL에 BSA의 3.3 mg을 디졸브.</li>
	<li>0.25 M의 재고 솔루션 tris(2-carboxyethyl) HPLC 물의 1 mL에서의 TCEP 62.5 mg를 용 해 하 여 phosphine (TCEP).</li>
	<li>TCEP의 최종 농도 8 m m까지 재고 TCEP 솔루션 반응 유리병에 추가 합니다.</li>
	<li>50 ° c.에 1 시간을 위한 물 욕조에 솔루션을 품 어 자력 교 반기를 사용 하 여 500 rpm에서 저 어.</li>
	<li>실내 온도에 완전히 냉각 솔루션을 수 있습니다.</li>
	<li>12.5 mg NEM의 HPLC 학년 물 1 mL에 용 해 하 여 100mm NEM의 재고 솔루션을 준비 합니다.</li>
	<li>NEM의 최종 농도 16 m m까지 반응 유리병에 NEM의 재고 솔루션을 추가 합니다.</li>
	<li>솔루션 2 h 20 ° c.에 대 한 결합을 허용합니다 500 rpm에서 저 어.</li>
	<li>초과 TCEP, NEM, 및 요소를 제거 하는 50mm NH4HCO3 의 500 mL에서 하룻밤 자력으로 50 rpm에서 솔루션을 저 어 12 kDa 투 석 튜브를 사용 하 여 솔루션 dialyze</li>
	<li>37 ° C에 물 목욕을 반응 유리병을 이동 하 고 750 rpm에서 저 어.</li>
	<li>0.66 m m의 농도를 HPLC 학년 물 산 성 chloroauric를 분해.</li>
	<li>즉시 반응 유리병에 chloroauric 산 성 해결책의 1 mL을 추가 하 고 2 분 대 혼합을 허용.</li>
	<li>해결책의 pH는 12까지 1 M NaOH를 추가 하 고 2 시간에 대 한 혼합 계속 솔루션을 허용.</li>
</ol>

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A. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Copper-Binding+Properties+of+Bovine+Serum+Albumin+and+Its+Amino-terminal+Peptide+Fragment.">Copper-Binding Properties of Bovine Serum Albumin and Its Amino-terminal Peptide Fragment.</a> Journal of Biological Chemistry. 242, 1574-1578 (1967).</li><li>Xue, Y., Li, X., Li, H., Zhang, W. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=Quantifying+Thiol-Gold+Interactions+towards+the+Efficient+Strength+Control.">Quantifying Thiol-Gold Interactions towards the Efficient Strength Control.</a> Nature Communications. 5, 4348 (2014).</li><li>Xu, Y., et al. <a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Search&doptcmdl=Citation&defaultField=Title+Word&term=The+Role+of+Protein+Characteristics+in+the+Formation+and+Fluorescence+of+Au+Nanoclusters.">The Role of Protein Characteristics in the Formation and Fluorescence of Au Nanoclusters.</a> Nanoscale. 6 (3), 1515-1524 (2014).</li></ol>

저자는 공개 없다.

PH 12에서 BSA-Au(III) 화합물 λ그들의 방출 파장에 빨간색 형광을 전시 = 640 nm로 자외선 (UV) 빛 λ전= 365 nm (그림 1A). 빨간 형광의 출현은 느린 과정이 고 최대 강도를 높이기 위해 실내 온도에 몇 일을 걸릴 것입니다. 37 ° C에서 반응 실행 높은 온도 빨리 빨간 형광을 생산 하 사용할 수 있습니다 최적의 결과 얻을 것 이다. 단백질의 돌이킬 수 없는 저하<sup c...

BSA-Au 화합물 전시는 자외선 (UV)-놀라운와 고르기 빨간색 형광 shift 스톡 스, 시 외원래 합성. 1. 고유 하 고 고정적 빨간 형광2,3,4,5,,67이미징 또는 nanomedicine8 감지 분야에서 다양 한 응용 프로그램을 찾을 수 있습니다 ,,910,11,,1213. 이 화합물은 최근 몇 년 동안14,,1516나노 과학의 분야에서 많은 연구자에 의해 광범위 하 게 공부 되었습니다 했다. BSA-Au 화합물 Au25 nanoclusters로 해석 되었습니다. 제시 방법의 목표는 세부에서이 화합물을 확인 하 고 빨간 형광의 기원 이해를 이다. 제시 방법에 따라, 여러 Au 바인딩 사이트의 존재 그리고 형광, Au25 nanoclusters의 단일 사이트 nucleation 대안의 기원 그림 될 수 있습니다. 동일한 접근은 다른 단백질17,,1819 complexed Au(III)와 그들의 본질적인 형광 속성을 변경할 수 있습니다 어떻게 연구 하 사용할 수 있습니다.
레드-형광 BSA Au 화합물의 합성에는 au (BSA:Au) 여기 방출 지도 (EEM)20에 봉우리의 위치는 형광의 강도 극대화 하는 BSA의 어 금 니 비율의 좁은 제어를 필요 합니다. 그것은 수 표시 여러 바인딩 사이트에 바인딩하려면 Au(III)에 대 한 존재는 아스파라긴 조각 (또는 Asp 조각, BSA의 N-말단에서 처음 4 개의 아미노산 잔류물)를 포함 하 여21,22. BSA (Cys-34)의 34번째 아미노산 Au(III)를 조정 하 고 레드 fluorescence([Cys34-capped-BSA]-Au(III))20의 구조에 참여 하는 것에 표시 됩니다. 모든 Cys Cys 이황화 결합을 고착 하 고 모든 thiols, 빨간색 형광 상한 시은 생산된 ([all-thiol-capped-BSA]-Au(III)). 이 빨간 형광을 생산 하는 Au(III) 바인딩 사이트 Cys Cys 이황화 결합의 필요성을 나타냅니다.
단백질 화학 기법은 하지 널리 나노 과학 커뮤니티에서 BSA-Au(III) 단지 공부를 사용 되었습니다. 그러나, 그것은이 단지, 또한 BSA에서 Au(III) 바인딩 사이트의 상세한 이해로 특정 측면을 이해 하는이 기법을 채택 하는 귀중 한 것입니다. 이 문서는 이러한 기술 중 일부를 보여 것입니다.

<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), &gt;99.0%</td><td>Sigma-Aldrich</td><td>4259</td><td></td></tr><tr><td>Tris(2-carboxyethyl)phosphine hydrochloride (TCEP), &gt;98.0%</td><td>Sigma-Aldrich</td><td>C4706</td><td></td></tr><tr><td>Sodium hydroxide, &gt;98.0%</td><td>Sigma-Aldrich</td><td>S8045</td><td></td></tr><tr><td>Urea, 99.5%</td><td>Chem-Implex Int&#039;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)

제시 프로토콜의 목적은 Au(III) 바인딩할 구조 변화 유도 빨간색 형광 저조한 BSA의 과정을 공부 하는 (λem = 640 nm) BSA-Au(III) 복합물의. 메서드를 사용 하면 pH 빨간색 형광의 출현을 BSA conformations의 pH 유도 평형 전환 연관 표시를 조정 합니다. 빨간 형광 BSA-Au(III) 단지는 pH 9.7, 이상 해당 BSA의 "양식" 나 란 하의 조정만 형성 수 있습니다. 누구나 어 금 니 비율을 BSA를 조정 하 고 Au(III) 바인딩 과정의 시간 과정을 모니터를 프로토콜 설명 되어 있습니다. 빨간 형광을 생산 하기 위해 BSA 당 Au(III)의 최소 수 미만 7 이다. 우리는 BSA에 여러 Au(III) 바인딩 사이트의 존재를 설명 하는 단계에서 프로토콜을 설명 합니다. 구리를 추가 하 여 첫 번째 (Cu(II)) 또는 니켈 (Ni(II)) 양이온 Au(III) 다음,이 방법을 보여준다 바인딩 사이트 빨간 fluorophore는 Au(III)에 대 한. 둘째, thiol 에이전트를 상한 하 여 BSA를 수정 하 여 다른 nonfluorophore 형성 Au(III) 바인딩 사이트가 드러났습니다. 셋째, 가능한 Au(III) 바인딩 사이트 고착 및 이황화 결합의 상한 BSA 구조 변경, 그림은. 프로토콜 설명, BSA conformations 및 Au(III) 바인딩을 제어 하는 다른 단백질 및 금속 양이온의 상호 작용을 공부 하 일반적으로 적용할 수 있습니다.

BSA-Au(III) 복합물의 형광에서 관찰 되었다 하는 BSA의 본질적인 파란 형광의 변환 (λem = 400 nm) 빨간색 형광을 (λem = 640 nm) 평형 통해 pH 9.7에 대해 발생 합니다 전환 (그림 1)입니다. EEM BSA-Au(III) Au 어 금 니 비율에 다른 BSA에 그림 2에 표시 하 고이 데이터 어떻게 다른 여기 파장에서 같은 방출 파장을 생...

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

골드 양이온 (소 혈 청 알 부 민 (BSA) 구조적 종속 독특한 BSA Au 형광 특성화에 관해서는 잘 제시의 다양 한 conformations 하 Au(III))의 바인딩 공부에 대 한 프로토콜.

Gold(III)의 바인딩에 의해 소 혈 청 알 부 민의 다양 한 Conformations에 Luminophore 형성

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)

6.8K 조회수.  University of North Carolina. 골드 양이온 (소 혈 청 알 부 민 (BSA) 구조적 종속 독특한 BSA Au 형광 특성화에 관해서는 잘 제시의 다양 한 conformations 하 Au(III))의 바인딩 공부에 대 한 프로토콜.

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

Synthetic Methodology for Asymmetric Ferrocene Derived Bio-conjugate Systems via Solid Phase Resin-based Methodology

Early detection is a key to successful treatment of most diseases, and is particularly imperative for the diagnosis and treatment of many types of cancer. The most common techniques utilized are imaging modalities such as Magnetic Resonance Imaging (MRI), Positron Emission Topography (PET), and Computed Topography (CT) and are optimal for understanding the physical structure of the disease but can only be performed once every four to six weeks due to the use of imaging agents and overall cost. With this in mind, the development of &#8220;point of care&#8221; techniques, such as biosensors, which evaluate the stage of disease and/or efficacy of treatment in the clinician&#8217;s office and do so in a timely manner, would revolutionize treatment protocols.1 As a means to exploring ferrocene based biosensors for the detection of biologically relevant molecules2, methods were developed to produce ferrocene-biotin bio-conjugates described herein. This report will focus on a biotin-ferrocene-cysteine system that can be immobilized on a gold surface.

The synthesis of asymmetric species of ferrocene is challenging using solution techniques. This report focuses on the methods carried out to produce a ferrocene-biotin bioconjugate using facile and clean reactions accomplished via solid-phase synthesis. Incorporation of a thiolate moiety is shown to impart the ability for immobilization on gold surfaces.

고상 수지 기반의 방법론을 통해 비대칭 페로센 유래 바이오 복합체 시스템 용 합성 방법론

Early detection is a key to successful treatment of most diseases, and is particularly imperative for the diagnosis and treatment of many types of cancer. ...

연구

화학

Iridium(III) Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II

This work outlines the synthesis of a non-emissive, cyclometalated Ir(III) complex, Ir(ppy)2(H2O)2+ (Ir1), which elicits a rapid, long-lived phosphorescent signal when coordinated to a histidine-containing protein immobilized on the surface of a magnetic particle. Synthesis of Ir1, in high yields,is complete O/N&#160;and involves splitting of the parent cyclometalated Ir(III) chloro-bridged dimer into two equivalents of the solvated complex. To confirm specificity, several amino acids were probed for coordination activity when added to the synthesized probe, and only histidine elicited a signal response. Using BNT-II, a branched peptide mimic of the malarial biomarker Histidine Rich Protein II (pfHRP-II), the iridium probe was validated as a tool for HRP-II detection. Quenching effects were noted in the BNT-II/Ir1 titration when compared to L-Histidine/Ir1, but these were attributed to steric hindrance and triplet state quenching. Biolayer interferometry was used to determine real-time kinetics of interaction of Ir1 with BNT-II. Once the system was optimized, the limit of detection of rcHRP-II using the probe was found to be 12.8 nM in solution. When this protein was immobilized on the surface of a 50 &#181;m magnetic agarose particle, the limit of detection was 14.5 nM. The robust signal response of this inorganic probe, as well as its flexibility of use in solution or immobilized on a surface, can lend itself toward a variety of applications, from diagnostic use to imaging.

IridiumIII Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II

Robust detection reagents are of increasing necessity for developing new malaria diagnostic tools. An iridium(III) probe was designed that emits long-lasting luminescent signal in the presence of a histidine-rich malarial protein biomarker. Detection of the protein either in solution or immobilized on a magnetic particle affords flexibility in application.

말라리아 단백질 바이오 마커 히스티딘 풍부한 단백질-II의 검출을위한 이리듐 (III) 발광 프로브

This work outlines the synthesis of a non-emissive, cyclometalated Ir(III) complex, Ir(ppy)2(H2O)2+ (Ir1), which elicits a rapid, long-lived ...

Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies

In this publication the gold sorption behavior of surface layer (S-layer) proteins (Slp1) of Lysinibacillus sphaericus JG-B53 is described. These biomolecules arrange in paracrystalline two-dimensional arrays on surfaces, bind metals, and are thus interesting for several biotechnical applications, such as biosorptive materials for the removal or recovery of different elements from the environment and industrial processes. The deposition of Au(0) nanoparticles on S-layers, either by S-layer directed synthesis 1 or adsorption of nanoparticles, opens new possibilities for diverse sensory applications. Although numerous studies have described the biosorptive properties of S-layers 2-5, a deeper understanding of protein-protein and protein-metal interaction still remains challenging. In the following study, inductively coupled mass spectrometry (ICP-MS) was used for the detection of metal sorption by suspended S-layers. This was correlated to measurements of quartz crystal microbalance with dissipation monitoring (QCM-D), which allows the online detection of proteinaceous monolayer formation and metal deposition, and thus, a more detailed understanding on metal binding.
The ICP-MS results indicated that the binding of Au(III) to the suspended S-layer polymers is pH dependent. The maximum binding of Au(III) was obtained at pH 4.0. The QCM-D investigations enabled the detection of Au(III) sorption as well as the deposition of Au(0)-NPs in real-time during the in situ experiments. Further, this method allowed studying the influence of metal binding on the protein lattice stability of Slp1. Structural properties and protein layer stability could be visualized directly after QCM-D experiment using atomic force microscopy (AFM). In conclusion, the combination of these different methods provides a deeper understanding of metal binding by bacterial S-layer proteins in suspension or as monolayers on either bacterial cells or recrystallized surfaces.

Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies

To obtain basic information on the sorption and recycling of gold from aqueous systems the interaction of Au(III) and Au(0) nanoparticles on S-layer proteins were investigated. The sorption of protein polymers was investigated by ICP-MS and that of proteinaceous monolayers by QCM-D. Subsequent AFM enables the imaging of the nanostructures.

Slp1 중합체 및 단층의 AU-상호 작용<em&gt; Lysinibacillus 스패 리 쿠스</em&gt; JG-B53 - QCM-D, 생체 분자 - 금속 연구 도구로서 ICP-MS와 AFM

In this publication the gold sorption behavior of surface layer (S-layer) proteins (Slp1) of Lysinibacillus sphaericus JG-B53 is described. These ...

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Cell proteomes are often characterized using electrophoresis assays, where all species of proteins in the cells are non-specifically labeled with a fluorescent dye and are spotted by a photodetector following their separation. Single molecule fluorescence imaging can provide ultrasensitive protein detection with its ability for visualizing individual fluorescent molecules. However, the application of this powerful imaging method to electrophoresis assays is hampered by the lack of ways to characterize the homogeneity of fluorescent labeling of each protein species across the proteome. Here, we developed a method to evaluate the labeling homogeneity across the proteome based on a single molecule fluorescence imaging assay. In our measurement using a HeLa cell sample, the proportion of proteins labeled with at least one dye, which we termed &#8216;labeling occupancy&#8217; (LO), was determined to range from 50% to 90%, supporting the high potential of the application of single molecule imaging to sensitive and precise proteome analysis.

Here, we present a protocol to assess the labeling homogeneity for each protein species in a complex protein sample at the single molecule level.

단일 분자 수준에서 동질성을 라벨의 프로테옴 와이드 정량화

Cell proteomes are often characterized using electrophoresis assays, where all species of proteins in the cells are non-specifically labeled with a ...

생화학

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening

We demonstrate a new drug screening method for determining the binding affinity of small drug molecules to a target protein by forming fluorescent gold nanoclusters (Au NCs) within the drug-loaded protein, based on the differential fluorescence signal emitted by the Au NCs. Albumin proteins such as human serum albumin (HSA) and bovine serum albumin (BSA) are selected as the model proteins. Four small molecular drugs (e.g., ibuprofen, warfarin, phenytoin, and sulfanilamide) of different binding affinities to the albumin proteins are tested. It was found that the formation rate of fluorescent Au NCs inside the drug loaded albumin protein under denaturing conditions (i.e., 60 &#176;C or in the presence of urea) is slower than that formed in the pristine protein (without drugs). Moreover, the fluorescent intensity of the as-formed NCs is found to be inversely correlated to the binding affinities of these drugs to the albumin proteins. Particularly, the higher the drug-protein binding affinity, the slower the rate of Au NCs formation, and thus a lower fluorescence intensity of the resultant Au NCs is observed. The fluorescence intensity of the resultant Au NCs therefore provides a simple measure of the relative binding strength of different drugs tested. This method is also extendable to measure the specific drug-protein binding constant (KD) by simply varying the drug content preloaded in the protein at a fixed protein concentration. The measured results match well with the values obtained using other prestige but more complicated methods.

A protocol for small molecular drug screening based on in-situ synthesis of ultrasmall fluorescent gold nanoclusters (Au NCs) using drug-loaded protein as template is presented. This method is simple to determine the binding affinity of drugs to a target protein by a visible fluorescent signal emitted from the protein-templated Au NCs.

단백질 표적 소분자 약물 검사를위한 신속하고 정량적적인 형광 방법

We demonstrate a new drug screening method for determining the binding affinity of small drug molecules to a target protein by forming fluorescent gold ...

생체공학

Determining Total Protein and Bioactive Protein Concentrations in Bovine Colostrum

Colostrum is a complex biological fluid produced by mammals immediately after parturition. It meets all the nutritional requirements for neonates as a good source of macro- and micronutrients, bioactive peptides, and growth factors. Bovine colostrum is also a potential source of nutrition and bioactive because of its rich protein content that includes immunoglobulin G (IgG) and lactoferrin. However, the level of lactoferrin and IgG in bovine colostrum changes markedly during the lactation period. Therefore, monitoring the concentration of IgG and lactoferrin for the use of bovine colostrum as a protein source is an important question to study. Methods in this article describe how to determine protein content, as well as specific concentrations of lactoferrin and IgG. These methods include the following steps: Isolation of bovine colostrum proteins, Determination of protein concentration via Bicinchoninic acid assay (BCA), Visualization of proteins via SDS-PAGE, Determination of lactoferrin, and IgG concentration using an ELISA Assay.

Bovine colostrum is both a primary source of nutrients and immunological support for the newborn calf. The understanding of the level of therapeutic proteins (lactoferrin and IgG) is important for the bovine colostrum dosing and standardization for human consumption.

Colostrum is a complex biological fluid produced by mammals immediately after parturition. It meets all the nutritional requirements for neonates as a ...

Limited Proteolysis and Gel Electrophoresis in the Presence of Metal Cations: Au(III)-binding Luminescent Domain in Serum Albumins

The purpose of the presented protocols is to determine the domain of Au(III) binding in BSA. The BSA-Au(III) compound exhibits ultraviolet (UV)-excitable red luminescence (&#955;em = 640 nm), with unusual Stokes shifts compared to the innate UV/blue fluorescence arising from the aromatic residues. Red-luminescent complexes are formed in highly alkaline conditions above pH 10 and require a conformation change within the protein to occur. In addition, preservation of Cys-Cys disulfide bonds in BSA is necessary to obtain this red luminescence. In order to understand the mechanism of this luminescence, elucidation of the luminophore-forming Au(III) binding site is essential. A facile way to assess the luminophore-forming site would be to (1) predictably fragment the protein by enzymatic digestion, (2) react the obtained fragments with Au(III), then (3) perform gel electrophoresis to observe the well-separated fragment bands and analyze the in-gel red luminescence. However, due to the alkaline conditions and the reaction with metal cations, new limited proteolysis techniques and gel electrophoresis conditions must be applied. Particularly, the presence of metal cations in gel electrophoresis can make the band separations technically difficult. We describe this new protocol in steps to identify the red-luminophore-forming metal binding domain in BSA. This protocol can thus be applied for analyzing protein fragments that must remain in a non-denatured or a partially denatured state, in the presence of metal cations. Because the majority of proteins need metal cations to function, analyses of metal-bound proteins are often desired, which have relied on x-ray crystallography in the literature. This method, on the other hand, could be used in supplement to study the interactions of proteins with metal cations without requiring the protein crystallization and at a desired pH condition.

Limited Proteolysis and Gel Electrophoresis in the Presence of Metal Cations: AuIII-binding Luminescent Domain in Serum Albumins

We present a protocol for studying the binding domain of Au(III) in bovine serum albumin (BSA).

The purpose of the presented protocols is to determine the domain of Au(III) binding in BSA. The BSA-Au(III) compound exhibits ultraviolet (UV)-excitable ...

Synthesis of Near-Infrared Emitting Gold Nanoclusters for Biological Applications

Over the past decade, fluorescent gold nanoclusters (AuNCs) have witnessed growing popularity in biological applications and enormous efforts have been devoted to their development. In this protocol, a recently developed, facile method for preparation of water soluble, biocompatible, and colloidally stable near-infrared emitting AuNCs have been described in detail. This room-temperature, bottom-up chemical synthesis provides easily functionalizable AuNCs capped with thioctic acid and thiol-modified polyethylene glycol in aqueous solution. The synthetic approach requires neither organic solvents or additional ligand exchange nor extensive knowledge of synthetic chemistry to reproduce. The resulting AuNCs offer free surface carboxylic acids, which can be functionalized with various biological molecules bearing a free amine group without adversely affecting the photoluminescent properties of the AuNCs. A quick, reliable procedure for flow cytometric quantification and confocal microscopic imaging of AuNC uptake by HeLa cells also been described. Due to the large Stokes shift, proper setting of filters in flow cytometry and confocal microscopy is necessary for efficient detection of near-infrared photoluminescence of AuNCs.

A reliable and easily reproducible method for preparation of functionalizable, near-infrared emitting photoluminescent gold nanoclusters and their direct detection inside HeLa cells by flow cytometry and confocal laser scanning microscopy is described.

생물학적 응용 을 위한 근적외선 방출 금 나노클러스터의 합성

Over the past decade, fluorescent gold nanoclusters (AuNCs) have witnessed growing popularity in biological applications and enormous efforts have been ...

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

The characterization of A&#946;1-40 coated over the nano-gold colloidal particle surfaces was conducted using surface plasmon resonance (SPR) spectroscopy and transmission electron microscopy (TEM). The observed pH-dependent shift of the SPR band of A&#946;1-40-coated 20 nm gold particles was correlated with alternation of aggregation and disaggregation observed in the TEM images. A pH of ~4&#160;induced an unfolded conformation, and a pH of ~10&#160;induced a folded conformation of A&#946;1-40 on the gold surface. This reversible aggregation process was observed by Raman imaging as the pH was gradually changed from pH 4 to pH 10. We observed a pH-dependent morphology change in A&#946;1-40 on the gold surface, where clear aggregates were observed at pH 4. However, we observed very subtle differences in the surface-enhanced Raman spectroscopy (SERS) spectrum between pH 4 and pH 10 conditions, with the most striking difference being spectral density in the region of 250 cm-1 and 1750 cm-1. Specifically, the mode analysis of the reversible aggregation indicated that the aggregates were formed by the unfolded conformation of A&#946;1-40 which involved the benzene ring section of Tyrosine and Phenylalanine. Conversely, the disassembly of the aggregates was associated with conformational changes in protein folding of A&#946;1-40 involving Histidine, Glutamine, Methionine, and Aspartic acid.

Here, we present a systematic method describing the quasi-reversible self-assembly of the amyloid beta 1-40 (A&#946;1-40)-coated 20 nm gold aggregates. The nano-size-dependent quasi-reversible networking between peptides was correlated with specific amino acids or sections of the A&#946;1-40 monomer.

Amyloid Beta 1-40-Coated Gold Colloids의 pH 의존성 가역적 자가 조립의 특성화

The characterization of A&#946;1-40 coated over the nano-gold colloidal particle surfaces was conducted using surface plasmon resonance (SPR) spectroscopy ...

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer

FRET is a process whereby energy is non-radiatively transferred from an excited donor molecule to a ground-state acceptor molecule through long-range dipole-dipole interactions1. In the present sensing assay, we utilize an interesting property of PDA: blue-shift in the UV-Vis electronic absorption spectrum of PDA (Figure 1) after an analyte interacts with receptors attached to PDA2,3,4,7. This shift in the PDA absorption spectrum provides changes in the spectral overlap (J) between PDA (acceptor) and rhodamine (donor) that leads to changes in the FRET efficiency. Thus, the interactions between analyte (ligand) and receptors are detected through FRET between donor fluorophores and PDA. In particular, we show the sensing of a model protein molecule streptavidin. We also demonstrate the covalent-binding of bovine serum albumin (BSA) to the liposome surface with FRET mechanism. These interactions between the bilayer liposomes and protein molecules can be sensed in real-time. The proposed method is a general method for sensing small chemical and large biochemical molecules. Since fluorescence is intrinsically more sensitive than colorimetry, the detection limit of the assay can be in sub-nanomolar range or lower8. Further, PDA can act as a universal acceptor in FRET, which means that multiple sensors can be developed with PDA (acceptor) functionalized with donors and different receptors attached on the surface of PDA liposomes.

We demonstrate FRET between conjugated polymer polydiacetylene (PDA) and fluorophore attached to the surface of PDA liposomes for the sensing of biomolecules. PDA liposomes also contained receptor molecules on their surfaces for biomolecules to be used as probes. Ligand-receptor interactions lead to changes in the FRET efficiency between the fluorophore and PDA which is the basis of the sensing mechanism.

형광 공명 에너지 전송과 리간드 - 수용체 상호 작용의 실시간 모니터링

FRET is a process  whereby energy is non-radiatively transferred from an excited donor molecule to  a ground-state acceptor molecule through long-range ...