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A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides.

Publication ,  Journal Article
Nitz, M; Franz, KJ; Maglathlin, RL; Imperiali, B
Published in: Chembiochem : a European journal of chemical biology
April 2003

Lanthanide-binding tags (LBTs) are protein fusion partners consisting of encoded amino acids that bind lanthanide ions with high affinity. Herein, we present a new screening methodology for the identification of new LBT sequences with high affinity for Tb(3+) ions and intense luminescence properties. This methodology utilizes solid-phase split-and-pool combinatorial peptide synthesis. Orthogonally cleavable linkers allow an efficient two-step screening procedure. The initial screen avoids the interference caused by on-bead screening by photochemically releasing a portion of the peptides into an agarose matrix for evaluation. The secondary screen further characterizes each winning sequence in a defined aqueous solution. Employment of this methodology on a series of focused combinatorial libraries yielded a linear peptide sequence of 17 encoded amino acids that demonstrated a 140-fold increase in affinity (57 nM dissociation constant, K(D)) over previously reported lanthanide-binding peptides. This linear sequence was macrocyclized by introducing a disulfide bond between flanking cysteine residues to produce a peptide with a 2-nM apparent dissociation constant for Tb(3+) ions.Supporting information for this article is available on the WWW under http://www.chemphyschem.org or from the author.

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Published In

Chembiochem : a European journal of chemical biology

DOI

EISSN

1439-7633

ISSN

1439-4227

Publication Date

April 2003

Volume

4

Issue

4

Start / End Page

272 / 276

Related Subject Headings

  • Terbium
  • Recombinant Fusion Proteins
  • Protein Binding
  • Peptides
  • Peptide Library
  • Organic Chemistry
  • Molecular Sequence Data
  • Luminescent Measurements
  • Consensus Sequence
  • Combinatorial Chemistry Techniques
 

Citation

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Nitz, M., Franz, K. J., Maglathlin, R. L., & Imperiali, B. (2003). A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides. Chembiochem : A European Journal of Chemical Biology, 4(4), 272–276. https://doi.org/10.1002/cbic.200390047
Nitz, Mark, Katherine J. Franz, Rebecca L. Maglathlin, and Barbara Imperiali. “A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides.Chembiochem : A European Journal of Chemical Biology 4, no. 4 (April 2003): 272–76. https://doi.org/10.1002/cbic.200390047.
Nitz M, Franz KJ, Maglathlin RL, Imperiali B. A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides. Chembiochem : a European journal of chemical biology. 2003 Apr;4(4):272–6.
Nitz, Mark, et al. “A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides.Chembiochem : A European Journal of Chemical Biology, vol. 4, no. 4, Apr. 2003, pp. 272–76. Epmc, doi:10.1002/cbic.200390047.
Nitz M, Franz KJ, Maglathlin RL, Imperiali B. A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides. Chembiochem : a European journal of chemical biology. 2003 Apr;4(4):272–276.
Journal cover image

Published In

Chembiochem : a European journal of chemical biology

DOI

EISSN

1439-7633

ISSN

1439-4227

Publication Date

April 2003

Volume

4

Issue

4

Start / End Page

272 / 276

Related Subject Headings

  • Terbium
  • Recombinant Fusion Proteins
  • Protein Binding
  • Peptides
  • Peptide Library
  • Organic Chemistry
  • Molecular Sequence Data
  • Luminescent Measurements
  • Consensus Sequence
  • Combinatorial Chemistry Techniques