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Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity

: Hüttl, C.; Hettrich, C.; Miller, R.; Paulke, B.-R.; Henklein, P.; Rawel, H.; Bier, F.F.

Fulltext ()

BMC biotechnology. Online journal 13 (2013), Article 51
ISSN: 1472-6750
Journal Article, Electronic Publication
Fraunhofer IAP ()
Fraunhofer IBMT ()

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.