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@ARTICLE{Hoffmann:9747,
author = {Hoffmann, S. and Funke, S. A. and Wiesehan, K. and Moedder,
S. and Glück, J.M. and Feuerstein, S.E. and Gerdts, J. and
Moetter, J. and Willbold, D.},
title = {{C}ompetitively selected protein ligands pay their increase
in specificity by a decrease in affinity},
journal = {Molecular BioSystems},
volume = {6},
issn = {1742-206X},
address = {Cambridge},
publisher = {Royal Society of Chemistry},
reportid = {PreJuSER-9747},
pages = {126 - 133},
year = {2010},
note = {Record converted from VDB: 12.11.2012},
abstract = {Protein-ligand interactions characterise and govern the
current state and fate of a living cell. The specificity of
proteins is mainly determined by the relative affinities to
each potential ligand. To investigate the consequences and
potentials of ligands with increased specificity in
comparison with ligands optimised solely for affinity, it
was necessary to identify ligands that are optimised towards
specificity instead of a barely optimised affinity to a
given target. In the presented example, a modified phage
display screening procedure yielded specific ligands for the
LckSH3 domain. We found that increased specificity of one of
the hereby obtained ligands for LckSH3 is achieved at the
cost of a slightly reduced affinity to LckSH3 and a
drastically reduced affinity to other SH3 domains. A surface
plasmon resonance experiment simulating in vivo-like
realistic competitive binding conditions exerted enhanced
binding behaviour of the specific ligand under these binding
conditions. The experimental data, together with a
mathematical model describing the complex experimental
situation, and theoretical considerations lead to the
conclusion that increased specificity is achieved at the
cost of reduced affinity, but after all, it pays if the
ligand is applied under realistic, i.e. competitive,
conditions.},
keywords = {Binding Sites: genetics / Binding Sites: physiology /
Ligands / Peptide Library / Protein Binding / Proteins:
chemistry / Proteins: metabolism / Surface Plasmon Resonance
/ src Homology Domains: genetics / src Homology Domains:
physiology / Ligands (NLM Chemicals) / Peptide Library (NLM
Chemicals) / Proteins (NLM Chemicals) / J (WoSType)},
cin = {ISB-3 / JARA-HPC},
ddc = {540},
cid = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
pnm = {Funktion und Dysfunktion des Nervensystems / BioSoft:
Makromolekulare Systeme und biologische
Informationsverarbeitung},
pid = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:20024074},
UT = {WOS:000272875200015},
doi = {10.1039/b910945e},
url = {https://juser.fz-juelich.de/record/9747},
}