Unraveling the origin of chirality from plasmonic nanoparticle-protein complexes

Author:

Zhang Qingfeng12ORCID,Hernandez Taylor1ORCID,Smith Kyle W.1ORCID,Hosseini Jebeli Seyyed Ali3ORCID,Dai Alan X.4ORCID,Warning Lauren1,Baiyasi Rashad3,McCarthy Lauren A.1ORCID,Guo Hua5ORCID,Chen Dong-Hua6,Dionne Jennifer A.7,Landes Christy F.123ORCID,Link Stephan123ORCID

Affiliation:

1. Department of Chemistry, Rice University, Houston, TX, USA.

2. Smalley-Curl Institute, Rice University, Houston, TX, USA.

3. Department of Electrical and Computer Engineering, Rice University, Houston, TX, USA.

4. Department of Chemical Engineering, Stanford University, Stanford, CA, USA.

5. Department of Materials Science and Nanoengineering, Rice University, Houston, TX, USA.

6. Department of Structural Biology, Stanford University, Stanford, CA, USA.

7. Department of Materials Science and Engineering, Stanford University, Stanford, CA, USA.

Abstract

Probing protein-nanorod aggregates The interaction of proteins with nanoparticles can enhance circular dichroism signals and provide a route for sensitive biodetection. However, ensemble measurements are insufficient for resolving the origin of plasmon-coupled circular dichroism (PCCD). Zhang et al. used single-particle circular differential scattering spectroscopy along with correlated tomographic reconstruction and electromagnetic simulations to study individual aggregates of bovine serum albumin and gold nanorods (see the Perspective by Kim and Kotov). Aggregates contribute to PCCD activity through formation of plasmonic hotspots, but single nanoparticles do not contribute. The protein does not function simply as a chiral chromophore but enables assembly of the chiral nanorod-protein complexes. Science , this issue p. 1475 ; see also p. 1378

Funder

National Science Foundation

Welch Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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