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Development of Peptidyl Lysine Dendrons: 1,3‐Dipolar Cycloaddition for Peptide Coupling and Antibody Recognition
Author(s) -
Hüttl Christine,
Hettrich Cornelia,
Riedel Melanie,
Henklein Petra,
Rawel Harshadrai,
Bier Frank F.
Publication year - 2015
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12444
Subject(s) - dendrimer , peptide , chemistry , combinatorial chemistry , click chemistry , surface plasmon resonance , peptide library , lysine , ligand (biochemistry) , peptide synthesis , solid phase synthesis , stereochemistry , peptide sequence , biochemistry , amino acid , nanotechnology , nanoparticle , materials science , receptor , gene
A straightforward synthesis strategy to multimerize a peptide mimotopes for antibody B13‐ DE 1 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 B 13‐ DE 1 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.