@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{HuettlHettrichRiedeletal.2015,
  author    = {H{\"u}ttl, Christine and Hettrich, Cornelia and Riedel, Melanie and Henklein, Petra and Rawel, Harshadrai Manilal and Bier, Frank Fabian},
  title     = {Development of Peptidyl Lysine Dendrons: 1,3-Dipolar Cycloaddition for Peptide Coupling and Antibody Recognition},
  series = {Chemical biology \& drug design},
  volume    = {85},
  journal   = {Chemical biology \& drug design},
  number    = {5},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1747-0277},
  doi       = {10.1111/cbdd.12444},
  pages     = {565 -- 573},
  year      = {2015},
  abstract  = {A straightforward synthesis strategy to multimerize a peptide mimotopes for antibody B13-DE1 recognition is described based on lysine dendrons as multivalent scaffolds. Lysine dendrons that possess N-terminal alkyne residues at the periphery were quantitative functionalized with azido peptides using click chemistry. The solid-phase peptide synthesis (SPPS) allows preparing the peptide dendron in high purity and establishing the possibility of automation. The presented peptide dendron is a promising candidate as multivalent ligand and was used for antibody B13-DE1 recognition. The binding affinity increases with higher dendron generation without loss of specificity. The analysis of biospecific interaction between the synthesized peptide dendron and the antibody was done via surface plasmon resonance (SPR) technique. The presented results show a promising tool for investigations of antigen-antibody reactions.},
  language  = {en}
}