Nanoencapsulation of ultra-small superparamagnetic particles of iron oxide into human serum albumin nanoparticles

• Matthias G. Wacker,
• Mahmut Altinok,
• Stephan Urfels and
• Johann Bauer

Beilstein J. Nanotechnol. 2014, 5, 2259–2266, doi:10.3762/bjnano.5.235

• Technische Universität Darmstadt, Technical Chemistry, D-64287 Darmstadt, Germany Merck KGaA, D-64287 Darmstadt, Germany 10.3762/bjnano.5.235 Abstract Human serum albumin nanoparticles have been utilized as drug delivery systems for a variety of medical applications. Since ultra-small superparamagnetic

• systemic exposition of patients with the carrier [6]. Human serum albumin (HSA) represents a promising candidate that binds a wide range of compounds with different physicochemical characteristics. In 2007, with Abraxane®, a first polymeric nanoparticle formulation consisting of this material has been

• time range. After freeze drying, only USPIO HSA hybrid particles prepared at an iron concentration of 15 µg/mg demonstrated significant agglomeration. Experimental Reagents and chemicals Human serum albumin (Fraction V) and glutaraldehyde 8% aqueous solution were purchased from Sigma (Steinheim

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

• reliable in our hands. In our original FCS study [45], we investigated the adsorption of human serum albumin (HSA) onto carboxyl-functionalized, polymer-encased iron platinum nanoparticles (Fe–Pt NPs) with a hydrodynamic radius, RH, of 5–6 nm. We prepared HSA solutions of different concentrations in

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

• 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

• 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