Phage display selection of miniprotein binders of the Estrogen Receptor

T. Phan; H. Nguyen; H. Göksel; S. Möcklinghoff; L. Brunsveld

doi:10.1039/C0CC02727H

Phage display selection of miniprotein binders of the Estrogen Receptor

T. Phan, H. Nguyen, H. Göksel, S. Möcklinghoff, L. Brunsveld

Chemical Biology

Research output: Contribution to journal › Article › Academic › peer-review

24 Citations (Scopus)

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Abstract

Miniprotein phage display screening yields structured peptides with high affinity for the Estrogen Receptor (ER). Hits from apamin phage libraries feature a LXXLL motif specifically placed on the predefined miniprotein helical segment. The apamin scaffold also allows optimization of flanking amino acids to ensure an optimal ER binding affinity

Original language	English
Pages (from-to)	8207-8209
Journal	Chemical Communications, ChemComm
Volume	46
Issue number	43
DOIs	https://doi.org/10.1039/C0CC02727H
Publication status	Published - 2010

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title = "Phage display selection of miniprotein binders of the Estrogen Receptor",

abstract = "Miniprotein phage display screening yields structured peptides with high affinity for the Estrogen Receptor (ER). Hits from apamin phage libraries feature a LXXLL motif specifically placed on the predefined miniprotein helical segment. The apamin scaffold also allows optimization of flanking amino acids to ensure an optimal ER binding affinity",

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AB - Miniprotein phage display screening yields structured peptides with high affinity for the Estrogen Receptor (ER). Hits from apamin phage libraries feature a LXXLL motif specifically placed on the predefined miniprotein helical segment. The apamin scaffold also allows optimization of flanking amino acids to ensure an optimal ER binding affinity

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Phage display selection of miniprotein binders of the Estrogen Receptor

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