Fast Self-Assembly Kinetics of Quantum Dots and a Dendrimeric Peptide Ligand

Wang, Jianhao; Jiang, Pengju; Han, Zuoyan; Qiu, Lin; Wang, Cheli; Zheng, Bo; Xia, Junfeng

doi:10.1021/la301227r

Cited by 48 publications

(61 citation statements)

References 26 publications

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“…The mechanism of metal-affinity-driven self-assembly of His-tagged proteins on the surface of GSH-coated CdSe/ZnS QDs could be described by a ligand displacement process. 11,12,26 The primary evidence is that both GSH and oligohistidine peptide (through the imidazole moiety of histidines) bind to the same binding sites on the ZnS shell of QDs, with GSH binding to Zn 2+ through Zn 2+ -S and Zn 2+ -N coordination bonds 27 and imidozole binding to Zn 2+ through the Zn 2+ -N coordination bond. 28 Therefore, GSH and oligohistidine (also imidazole) are competitive ligands for CdSe/ZnS QDs.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Genetically Encodable Design of Ligand “Bundling” on the Surface of Nanoparticles

Lu¹,

Wang²,

Wang

et al. 2012

Langmuir

Self Cite

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Polyhistidine peptide dendrimer self-assembles on CdSe/ZnS quantum dots (QDs) with very high affinity and stability, a property ascribable to its multivalent geometry. Here we designed a fluorescent protein, GCN-mCherry, that exists as an oligomeric bundled structure in solution as well as on the surface to imitate the structure of a synthetic dendrimer. GCN-mCherry forms a very stable assembly with QDs, which can resist displacement by 500 mM imidazole and the dendrimer peptide, as measured by the Förster resonance energy transfer from QD to mCherry. Our work manifested a prominent stability enhancement of protein-nanoparticle assembly through directional ligand-ligand interaction on the surface.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Genetically Encodable Design of Ligand “Bundling” on the Surface of Nanoparticles

Lu¹,

Wang²,

Wang

et al. 2012

Langmuir

Self Cite

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“…377 Wang et al used a microfluidic chip and FRET to study the binding kinetics between QDs and either a four-arm His n peptide dendrimer (PHPD) or a His 6 -terminated peptide with subsecond resolution. 283 Time correlated with the position of observation along the length of the microfluidic channel, as shown in Figure 134, permitting temporal resolution that would have been difficult with bulk solution measurements of changes in FRET. This type of assay format should be applicable for studying the kinetics of other types of binding events, such as that between a protein-QD conjugate and an acceptor-labeled ligand of that protein.…”

Section: Microfluidicsmentioning

confidence: 99%

Energy Transfer with Semiconductor Quantum Dot Bioconjugates: A Versatile Platform for Biosensing, Energy Harvesting, and Other Developing Applications

Spillmann²,

et al. 2016

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Luminescent semiconductor quantum dots (QDs) are one of the more popular nanomaterials currently utilized within biological applications. However, what is not widely appreciated is their growing role as versatile energy transfer (ET) donors and acceptors within a similar biological context. The progress made on integrating QDs and ET in biological configurations and applications is reviewed in detail here. The goal is to provide the reader with (1) an appreciation for what QDs are capable of in this context, (2) how this field has grown over a relatively short time span, and, in particular, (3) how QDs are steadily revolutionizing the development of new biosensors along with a myriad of other photonically active nanomaterial-based bioconjugates. An initial discussion of QD materials along with key concepts surrounding their preparation and bioconjugation is provided given the defining role these aspects play in the QDs ability to succeed in subsequent ET applications. The discussion is then divided around the specific roles that QDs provide as either Förster resonance energy transfer (FRET) or charge/electron transfer donor and/or acceptor. For each QD-ET mechanism, a working explanation of the appropriate background theory and formalism is articulated before examining their biosensing and related ET utility. Other configurations such as incorporation of QDs into multistep ET processes or use of initial chemical and bioluminescent excitation are treated similarly. ET processes that are still not fully understood such as QD interactions with gold and other metal nanoparticles along with carbon allotropes are also covered. Given their maturity, some specific applications ranging from in vitro sensing assays to cellular imaging are separated and discussed in more detail. Finally a perspective on how this field will continue to evolve is provided.

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“…While FRET can provide an optical signal for binding, a microfluidic chip can provide fast, efficient mixing with spatially resolved observation of the process. Droplet microfluidics is one such technology and has been combined with FRET to monitor the fast binding kinetics between a CdSe/ZnS core/shell quantum dot (QD) and a peptide appended with a dendritic tetra-hexahistidine motif [6]. Polyhistidine sequences spontaneously assemble to the ZnS shell, with equilibrium binding being reached within 100 s for a single hexahistidine sequence.…”

Section: Binding Kineticsmentioning

confidence: 99%

Fluorescence Resonance Energy Transfer (FRET)

Algar

2013

Encyclopedia of Microfluidics and Nanofluidics

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SynonymsElectronic energy transfer (EET); Förster resonance energy transfer (FRET) Definition Fluorescence resonance energy transfer (FRET) is a non-radiative, through-space excitation energy transfer process. The electronic excitation energy of a donor molecule is transferred to a ground-state acceptor through dipole-dipole interactions without involvement of a photon or molecular contact. Efficient FRET requires close proximity and suitable alignment between the transition dipoles of the donor and acceptor, as well as overlap between the donor emission spectrum and acceptor absorption spectrum. OverviewFRET was first elucidated by Theodor Förster between 1946 and 1948 [1]. Many researchers, including the International Union of Pure and Applied Chemistry (IUPAC), recognize FRET as Förster resonance energy transfer rather than fluorescence resonance energy transfer. The tribute to Förster notwithstanding, it is argued that the "fluorescence" terminology is incorrect because no photon is emitted during the energy transfer process. However, there is some value to the fluorescence resonance energy transfer terminology, which can be used to distinguish between energy transfer from optically excited donors and energy transfer from excited-state donors formed as the products of chemical or enzyme-catalyzed reactions. The latter two processes also follow the mechanism elucidated by Förster and are commonly referred to as chemiluminescence resonance energy transfer (CRET) and bioluminescence resonance energy transfer (BRET), respectively. In practice, both the "Förster" and "fluorescence" terminology are widely accepted expansions of the FRET acronym. Despite Förster's breakthrough in the mid-twentieth century, it was not until the 1990s that improvements in fluorescence instrumentation and the availability of fluorescent materials made it possible for the full potential of FRET to be realized [2]. Currently, FRET is one of the most powerful and widely utilized fluorescence techniques, with numerous applications in biology, biochemistry, biophysics, and bioanalysis.Physically, the FRET process is summarized in Eq. 1, where D represents the donor fluorophore, A represents the acceptor chromophore, and * indicates an excited electronic state.

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Fast Self-Assembly Kinetics of Quantum Dots and a Dendrimeric Peptide Ligand

Cited by 48 publications

References 26 publications

Genetically Encodable Design of Ligand “Bundling” on the Surface of Nanoparticles

Genetically Encodable Design of Ligand “Bundling” on the Surface of Nanoparticles

Energy Transfer with Semiconductor Quantum Dot Bioconjugates: A Versatile Platform for Biosensing, Energy Harvesting, and Other Developing Applications

Fluorescence Resonance Energy Transfer (FRET)

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