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Journal Article

Multiplexed sorting of libraries on libraries: A novel method for empirical protein design by affinity-driven phage enrichment on synthetic peptide arrays

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Hultschig,  Claus
Max Planck Society;

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Hultschig, C., & Frank, R. (2004). Multiplexed sorting of libraries on libraries: A novel method for empirical protein design by affinity-driven phage enrichment on synthetic peptide arrays. Molecular Diversity, 8(3), 231-245. doi:10.1023/B:MODI.0000036243.09027.a6.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-87E0-E
Abstract
Chemically synthesized peptide arrays on planar cellulosecarriers are proposed as libraries of ligands suitable for the multiplexedsimultaneous capture of peptide-specific acceptor proteins from a largerandomly mutagenized library of acceptor proteins presented onbacteriophage M13 particles. This experimental set-up can be exploited to rapidlyscreen for individual new, distinct binding partners from two complementarylibraries (two-dimensional screening). The technical feasibility of thisempirical protein design approach was demonstrated with calmodulin as anaceptor protein using an array of mastoparan variants for multiplexedphage affinity enrichment.