@article{HuettlHettrichMilleretal.2013,
  author    = {H{\"u}ttl, Christine and Hettrich, Cornelia and Miller, Reinhard and Paulke, Bernd-Reiner and Henklein, Petra and Rawel, Harshadrai Manilal and Bier, Frank Fabian},
  title     = {Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity},
  series = {BMC biotechnology},
  volume    = {13},
  journal   = {BMC biotechnology},
  number    = {22},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1472-6750},
  doi       = {10.1186/1472-6750-13-51},
  pages     = {10},
  year      = {2013},
  abstract  = {Background: A promising way in diagnostic and therapeutic applications is the development of peptide amphiphiles (PAs). Peptides with a palmitic acid alkylchain were designed and characterized to study the effect of the structure modifications on self-assembling capabilities and the multiple binding capacity to hemagglutinin (HA), the surface protein of influenza virus type A. The peptide amphiphiles consists of a hydrophilic headgroup with a biological functionality of the peptide sequence and a chemically conjugated hydrophobic tail. In solution they self-assemble easily to micelles with a hydrophobic core surrounded by a closely packed peptide-shell. Results: In this study the effect of a multiple peptide binding partner to the receptor binding site of HA could be determined with surface plasmon resonance measurements. The applied modification of the peptides causes signal amplification in relationship to the unmodified peptide wherein the high constant specificity persists. The molecular assembly of the peptides was characterized by the determination of critical micelle concentration (CMC) with concentration of 10(-5) M and the colloidal size distribution. Conclusion: The modification of the physico-chemical parameters by producing peptide amphiphiles form monomeric structures which enhances the binding affinity and allows a better examination of the interaction with the virus surface protein hemagglutinin.},
  language  = {en}
}
@article{CywinskiPietraszkiewiczMaciejczyketal.2016,
  author    = {Cywinski, Piotr J. and Pietraszkiewicz, Marek and Maciejczyk, Michal and Gorski, Krzysztof and Hammann, Tommy and Liermann, Konstanze and Paulke, Bernd-Reiner and L{\"o}hmannsr{\"o}ben, Hans-Gerd},
  title     = {Total protein concentration quantification using nanobeads with a new highly luminescent terbium(III) complex},
  series = {RSC Advances},
  volume    = {6},
  journal   = {RSC Advances},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2046-2069},
  doi       = {10.1039/c6ra23207h},
  pages     = {115068 -- 115073},
  year      = {2016},
  abstract  = {Total protein concentration (TPC) is a key parameter in many biochemical experiments and its quantification is often necessary for isolation, separation, and analysis of proteins. A sensitive and rapid nanobead-based TPC quantification assay based on Forster Resonance Energy Transfer (FRET) has been developed. A new, highly luminescent Tb(III) complex has been synthesised and applied as donor in this FRET assay with an organic dye (Cy5) as acceptor. FRET-induced changes in luminescence have been investigated both at donor and acceptor emission wavelength using time-resolved luminescence spectroscopy with time-gated detection. In the assay, the Tb(III) complex and fine-tuned polyglycidyl methacrylate (PGMA) nanobeads ensure that an improvement in sensitivity and background reduction is achieved. Using 40 nm large PGMA nanobeads loaded with the Tb(III) complex, it is possible to determine TPC down to 50 ng mL(-1) in just 10 minutes. Through specific assay components the sensitivity has been improved when compared to existing nanobead-based assays and to currently known commercial methods. Additionally, the assay is relatively insensitive to the presence of contaminants, such as non-ionic detergents commonly found in biological samples. Due to no need for any centrifugal steps, this mix-and-measure bioassay can easily be implemented into routine TPC quantification protocols in biochemical laboratories.},
  language  = {en}
}