Synthesis of triangular silver nanoprisms and spectroscopic analysis on the interaction with bovine serum albumin

Synthesis of triangular silver nanoprisms and spectroscopic analysis on the interaction with... The interactions of triangular silver nanoprisms (TAgNPrs) with bovine serum albumin (BSA) were investigated using multiple spectroscopic techniques. A noticeable absorbance increase was noted in the peak ranges of 250 to 300 nm for BSA, and the intensity increased with the increasing concentration of TAgNPrs. Furthermore, a slight blue shift of the surface plasmon resonance band of TAgNPrs occurred, indicating that the protein absorbed on the TAgNPrs surface to form a bio-nano interface. Analysis of fluorescence quenching data using the Stern-Volmer method revealed that static quenching takes place with complex formation. Evaluation of thermodynamic parameter ΔG θ for the binding processes indicated that the binding reaction was exothermic. Furthermore, the values of binding constant K revealed that the size of nanoparticles can affect the binding degree. The order of binding affinity is 43.7 nm > 36.2 nm > 25.1 nm. The competitive experiments of site markers (flufenamic acid and phenylbutazone) suggested that the binding site of TAgNPrs on BSA was located in the region of subdomain IIIA (Sudlow site II). In addition, the conformational changes of BSA by TAgNPrs were analyzed by using synchronous fluorescence spectra, circular dichroism, and three-dimensional fluorescence spectra. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Analytical and Bioanalytical Chemistry Springer Journals

Synthesis of triangular silver nanoprisms and spectroscopic analysis on the interaction with bovine serum albumin

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Publisher
Springer Berlin Heidelberg
Copyright
Copyright © 2017 by Springer-Verlag GmbH Germany
Subject
Chemistry; Analytical Chemistry; Biochemistry, general; Laboratory Medicine; Characterization and Evaluation of Materials; Food Science; Monitoring/Environmental Analysis
ISSN
1618-2642
eISSN
1618-2650
D.O.I.
10.1007/s00216-017-0478-4
Publisher site
See Article on Publisher Site

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