Recent advances in green carbon dots (2015–2022): synthesis, metal ion sensing, and biological applications

• Aisha Kanwal,
• Naheed Bibi,
• Sajjad Hyder,
• Arif Muhammad,
• Hao Ren,
• Jiangtao Liu and
• Zhongli Lei

Beilstein J. Nanotechnol. 2022, 13, 1068–1107, doi:10.3762/bjnano.13.93

• source). They showed that luminous impurities formed as byproducts during the synthesis of CDs mostly contribute to fluorescence emission by eliminating the molecular fluorophores [133]. By using fluorescence correlation spectroscopy and time-resolved electron paramagnetic resonance spectroscopy

Evaluation of quantum dot conjugated antibodies for immunofluorescent labelling of cellular targets

• Jennifer E. Francis,
• David Mason and
• Raphaël Lévy

Beilstein J. Nanotechnol. 2017, 8, 1238–1249, doi:10.3762/bjnano.8.125

• , we have provided our own measurements of Qdot 625 in the Supporting Information File 1. We attempted to measure the size of Qdot 625 using different methods: transmission electron microscopy (TEM), size-exclusion high-performance liquid chromatography (SEC-HPLC), and fluorescence correlation

• spectroscopy (FCS). The TEM and SEC-HPLC results are in agreement with the provider’s data, giving a core size of ≈8 nm (Figure S7 in Supporting Information File 1) and a hydrodynamic diameter of ≈15 nm (Figure S8 in Supporting Information File 1), respectively. However, the FCS results indicate a much larger

Protein corona – from molecular adsorption to physiological complexity

• Lennart Treuel,
• Dominic Docter,
• Michael Maskos and
• Roland H. Stauber

Beilstein J. Nanotechnol. 2015, 6, 857–873, doi:10.3762/bjnano.6.88

• acid (DHLA)-coated quantum dots (QDs) by using fluorescence correlation spectroscopy (FCS) [4]. The electrostatic surface potential of native HSA shows distinct, positively charged patches on an otherwise negative potential surface (Figure 3). These patches are caused by the presence of basic lysine

• protein fold was preserved. They then used fluorescence correlation spectroscopy to measure binding curves for the adsorption of native and modified HSA to DHLA-coated QDs. Intriguingly, these relatively simple chemical modifications of the proteins surface charge distribution, were found to dramatically

• American Chemical Society. Binding curves as determined by fluorescence correlation spectroscopy and schematic representations for adsorption of (a and b) HSA, (c and d) HSAsuc and (e and f) HSAam onto dihydrolipoic acid-coated quantum dots. Filled symbols: Hydrodynamic radii of DHLA-QDs plotted as a

The fate of a designed protein corona on nanoparticles in vitro and in vivo

• Denise Bargheer,
• Julius Nielsen,
• Gabriella Gébel,
• Markus Heine,
• Sunhild C. Salmen,
• Roland Stauber,
• Horst Weller,
• Joerg Heeren and
• Peter Nielsen

Beilstein J. Nanotechnol. 2015, 6, 36–46, doi:10.3762/bjnano.6.5

• . This is in agreement with earlier findings by Jiang et al. and Röcker et al. using smaller (10 nm) FePt-particles which had a similar coating [20][34]. They found by fluorescence correlation spectroscopy that both proteins adsorb onto the particles with affinities in the micromolar range (transferrin

Effects of surface functionalization on the adsorption of human serum albumin onto nanoparticles – a fluorescence correlation spectroscopy study

• Pauline Maffre,
• Stefan Brandholt,
• Karin Nienhaus,
• Li Shang,
• Wolfgang J. Parak and
• G. Ulrich Nienhaus

Beilstein J. Nanotechnol. 2014, 5, 2036–2047, doi:10.3762/bjnano.5.212

• Marburg, Renthof 7, 35037 Marburg, Germany, Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, IL 61801, USA 10.3762/bjnano.5.212 Abstract By using fluorescence correlation spectroscopy (FCS), we have studied the adsorption of human serum albumin (HSA) onto

• four orders of magnitude. These variations can be understood in terms of specific Coulombic interactions between the proteins and the NP surfaces. Keywords: fluorescence correlation spectroscopy; human serum albumin; nanoparticles; protein corona; quantum dots; Introduction In recent years, both

• respond to changes in the local protein concentration by desorption. Thus, only tightly bound proteins, with residence times on the NP surface much longer than the experimental time scale, will be quantified correctly. We have used fluorescence correlation spectroscopy (FCS) as a powerful method for the

In vitro interaction of colloidal nanoparticles with mammalian cells: What have we learned thus far?

• Moritz Nazarenus,
• Qian Zhang,
• Mahmoud G. Soliman,
• Pablo del Pino,
• Beatriz Pelaz,
• Susana Carregal-Romero,
• Joanna Rejman,
• Barbara Rothen-Rutishauser,
• Martin J. D. Clift,
• Reinhard Zellner,
• G. Ulrich Nienhaus,
• James B. Delehanty,
• Igor L. Medintz and
• Wolfgang J. Parak

Beilstein J. Nanotechnol. 2014, 5, 1477–1490, doi:10.3762/bjnano.5.161

• fluorescence correlation spectroscopy (FCS), Röcker et al. investigated the adsorption of human serum albumin onto FePt NPs and found clear evidence that the proteins formed a monolayer on the surface of the NP [136]. Additional FCS studies by using other important serum proteins invariably confirmed the

Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy

• Pauline Maffre,
• Karin Nienhaus,
• Faheem Amin,
• Wolfgang J. Parak and
• G. Ulrich Nienhaus

Beilstein J. Nanotechnol. 2011, 2, 374–383, doi:10.3762/bjnano.2.43

• , Renthof 7, 35037 Marburg, Germany, Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, IL 61801, USA 10.3762/bjnano.2.43 Abstract Using dual-focus fluorescence correlation spectroscopy, we have analyzed the adsorption of three human blood serum proteins

• understand the structural and dynamic properties of the protein corona at the molecular level. Recently, we have used quantitative fluorescence microscopy, especially fluorescence correlation spectroscopy (FCS), to study protein adsorption of human serum albumin (HSA) on polymer-coated FePt NPs with an

• correlation spectroscopy; human serum albumin; nanoparticle; protein adsorption; Introduction Recent years have seen enormous advances in the field of nanotechnology. A huge variety of nanoparticles (NPs), defined as objects with all three spatial dimensions in the range of 1–100 nm, has been developed, with