@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{AliHomannKhaliletal.2013,
  author    = {Ali, Mostafa and Homann, Thomas and Khalil, Mahmoud and Kruse, Hans-Peter and Rawel, Harshadrai Manilal},
  title     = {Milk whey protein modification by coffee-specific phenolics effect on structural and functional properties},
  series = {Journal of agricultural and food chemistry : a publication of the American Chemical Society},
  volume    = {61},
  journal   = {Journal of agricultural and food chemistry : a publication of the American Chemical Society},
  number    = {28},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0021-8561},
  doi       = {10.1021/jf402221m},
  pages     = {6911 -- 6920},
  year      = {2013},
  abstract  = {A suitable vehicle for integration of bioactive plant constituents is proposed. It involves modification of proteins using phenolics and applying these for protection of labile constituents. It dissects the noncovalent and covalent interactions of beta-lactoglobulin with coffee-specific phenolics. Alkaline and polyphenol oxidase modulated covalent reactions were compared. Tryptic digestion combined with MALDI-TOF-MS provided tentative allocation of the modification type and site in the protein, and an in silico modeling of modified beta-lactoglobulin is proposed. The modification delivers proteins with enhanced antioxidative properties. Changed structural properties and differences in solubility, surface hydrophobicity, and emulsification were observed. The polyphenol oxidase modulated reaction provides a modified beta-lactoglobulin with a high antioxidative power, is thermally more stable, requires less energy to unfold, and, when emulsified with lutein esters, exhibits their higher stability against UV light. Thus, adaptation of this modification provides an innovative approach for functionalizing proteins and their uses in the food industry.},
  language  = {en}
}