4.8 Article

Rotational and translational diffusion of peptide-coated CdSe/CdS/ZnS nanorods studied by fluorescence correlation spectroscopy

期刊

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 128, 期 5, 页码 1639-1647

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AMER CHEMICAL SOC
DOI: 10.1021/ja056162i

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资金

  1. NCRR NIH HHS [R01 RR014891-01, R01 RR014891, R01 RR014891-02, R01 RR014891-018271, R01 RR014891-01S1] Funding Source: Medline
  2. NIBIB NIH HHS [R01 EB000312-07, R01 EB000312-06A1, R01 EB000312-05, R01 EB000312, 5-R01 EB000312-04, R01 EB000312-03, R01 EB000312-04] Funding Source: Medline

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CdSe/CdS/ZnS nanorods (NRs) of three aspect ratios were coated with phytochelatin-related peptides and studied using fluorescence correlation spectroscopy (FCS). Theoretical predictions of the NRs' rotational diffusion contribution to the correlation curves were experimentally confirmed. We monitored rotational and translational diffusion of NRs and extracted hydrodynamic radii from the extracted diffusion constants. Translational and rotational diffusion constants (D-trans and D-rot) for NRs were in good agreement with Tirado and Garcia de la Torre's as well as with Broersma's theories when accounting for the ligand dimensions. NRs fall in the size range where rotational diffusion can be monitored with higher sensitivity than translational diffusion due to a steeper length dependence, D-rot similar to L-3 versus D-trans similar to L-1. By titrating peptide-coated NRs with bovine serum albumin, we monitored (nonspecific) binding through rotational diffusion and showed that D-rot is an advantageous observable for monitoring binding. Monitoring rotational diffusion of bioconjugated NRs using FCS might prove to be useful for observing binding and conformational dynamics in biological systems.

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