Stimuli-responsive polypeptide nanogels for trypsin inhibition

• Petr Šálek,
• Jana Dvořáková,
• Sviatoslav Hladysh,
• Diana Oleshchuk,
• Ewa Pavlova,
• Jan Kučka and
• Vladimír Proks

Beilstein J. Nanotechnol. 2022, 13, 538–548, doi:10.3762/bjnano.13.45

• substituents compared to PHEG-Tyr nanogel [25]. This assumption is also supported by the DH dependence (Figure 3a) showing a DH maximum at pH 7.4. Adsorption and release of BSA and AAT Next, optimization studies of in vitro loading of 125I-radiolabeled BSA as a model protein and its release from PHEG-Tyr and

• Nα-Lys-NG nanogels were performed. 125I-radiolabeled BSA was loaded onto PHEG-Tyr nanogel at pH 4.7 and 25 °C as PHEG-Tyr nanogel exhibits the most swollen state and a negative charge under these conditions (Figure 2). The uptake of BSA was found to be more efficient at or below the isoelectric point

• of BSA (pI 4.7) and, thus, BSA adsorption is driven by electrostatic and hydrophobic interactions [30][31]. PHEG-Tyr nanogel was incubated with three different 125I-radiolabeled BSA concentrations (1, 0.75, and 0.5 mg/mL), and the loading efficiency was found to be low, that is, 2.1% (21 µg/mL), 1.9

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

• surface was modified by PEGylation with mono- or bifunctional poly(ethylene oxide)amines (PEG). Using 125I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was studied first in vitro. Incubation with 125I-transferrin showed that with increasing grade of PEGylation

• proteins. If non-labeled transferrin was used as preformed corona and excess 125I-labeled albumin was added to the reaction mixtures with different SPIOs, a substantial amount of label was bound to the particles with initially adsorbed transferrin but little or even zero with covalently bound transferrin

• . These in vitro experiments show a clear difference in the stability of a preformed hard corona with adsorbed or covalently bound protein. This difference seems, however, to be of minor importance in vivo when polymer-coated 59Fe-SPIOs with adsorbed or covalently bound 125I-labeled mouse transferrin were