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

Onderzoeksoutput: Bijdrage aan tijdschrift › Tijdschriftartikel › Academic › peer review

27 Citaten (Scopus)

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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

Originele taal-2	Engels
Pagina's (van-tot)	8207-8209
Tijdschrift	Chemical Communications, ChemComm
Volume	46
Nummer van het tijdschrift	43
DOI's	https://doi.org/10.1039/C0CC02727H
Status	Gepubliceerd - 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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