2012Journal of Chemical Technology & BiotechnologyRequires access

Studies on the interaction of CdTe QDs with bovine serum albumin

Peng Liu, Yisi Liu, Qisui Wang

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Abstract

Abstract BACKGROUND:Quantum dots (QDs) have attracted much attention in biological and medical applications. In particular, the interaction of QDs with bovine serum albumin (BSA) is crucial, and has been systematically investigated by various spectroscopic techniques under the physiological conditions. RESULTS:The effects of ionic strength and pH on the interaction of CdTe QDs with BSA were studied by changing NaCl concentration and pH in mixed solution and making fluorescence spectroscopic measurements. The Stern‐Volmer quenching constant (Ka) of different ionic strength and pH were calculated, and information on the structural features of BSA were discussed by means of circular dichroism (CD) spectrum. CONCLUSION:Both fluorescence (FL) and circular dichroism (CD) results indicated that hydrophobic and electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs‐BSA complexes. Copyright © 2012 Society of Chemical Industry

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Abstract BACKGROUND:Quantum dots (QDs) have attracted much attention in biological and medical applications. In particular, the interaction of QDs with bovine serum albumin (BSA) is crucial, and has been systematically investigated by various spectroscopic techniques under the physiological conditions. RESULTS:The effects of ionic strength and pH on the interaction of CdTe QDs with BSA were studied by changing NaCl concentration and pH in mixed solution and making fluorescence spectroscopic measurements. The Stern‐Volmer quenching constant (Ka) of different ionic strength and pH were calculated, and information on the structural features of BSA were discussed by means of circular dichroism (CD) spectrum. CONCLUSION:Both fluorescence (FL) and circular dichroism (CD) results indicated that hydrophobic and electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs‐BSA complexes. Copyright © 2012 Society of Chemical Industry

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Available abstract

Abstract BACKGROUND:Quantum dots (QDs) have attracted much attention in biological and medical applications. In particular, the interaction of QDs with bovine serum albumin (BSA) is crucial, and has been systematically investigated by various spectroscopic techniques under the physiological conditions. RESULTS:The effects of ionic strength and pH on the interaction of CdTe QDs with BSA were studied by changing NaCl concentration and pH in mixed solution and making fluorescence spectroscopic measurements. The Stern‐Volmer quenching constant (Ka) of different ionic strength and pH were calculated, and information on the structural features of BSA were discussed by means of circular dichroism (CD) spectrum. CONCLUSION:Both fluorescence (FL) and circular dichroism (CD) results indicated that hydrophobic and electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs‐BSA complexes. Copyright © 2012 Society of Chemical Industry

Key concepts: Bovine serum albumin, Circular dichroism, Ionic strength, Quenching (fluorescence), Chemistry, Fluorescence, Quantum dot, Ionic bonding

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