Iterative In Situ Click Chemistry Creates Antibody-like Protein-Capture Agents

Special agents for protein capture: Iterative in situ click chemistry (see scheme for the tertiary ligand screen) and the one-bead-one-compound method for the creation of a peptide library enable the fragment-based assembly of selective high-affinity protein-capture agents. The resulting ligands are...

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Bibliographic Details
Published inAngewandte Chemie (International ed.) Vol. 48; no. 27; pp. 4944 - 4948
Main Authors Agnew, Heather D, Rohde, Rosemary D, Millward, Steven W, Nag, Arundhati, Yeo, Woon-Seok, Hein, Jason E, Pitram, Suresh M, Tariq, Abdul Ahad, Burns, Vanessa M, Krom, Russell J, Fokin, Valery V, Sharpless, K. Barry, Heath, James R
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 01.01.2009
WILEY‐VCH Verlag
Wiley
Subjects
Antibodies - chemistry
Catalysis
Chemistry
Chemistry, Multidisciplinary
click chemistry
combinatorial chemistry
Copper - chemistry
inhibitors
Ligands
Peptide Library
peptides
Peptides - chemistry
Physical Sciences
Protein Binding
Proteins - chemistry
protein‐capture agents
Science & Technology
Triazoles - chemistry
VITRO
inhibitors
CARBONIC-ANHYDRASE
ACIDS
HYDROLYSIS
click chemistry
peptides
APTAMER
MOLECULES
LIBRARIES
ACETYLCHOLINESTERASE
protein-capture agents
combinatorial chemistry
SELECTION
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Summary:Special agents for protein capture: Iterative in situ click chemistry (see scheme for the tertiary ligand screen) and the one-bead-one-compound method for the creation of a peptide library enable the fragment-based assembly of selective high-affinity protein-capture agents. The resulting ligands are water-soluble and stable chemically, biochemically, and thermally. They can be produced in gram quantities through copper(I)-catalyzed cycloaddition.
Bibliography:http://dx.doi.org/10.1002/anie.200900488
This research was supported by the National Cancer Institute, grant No. 5U54 CA119347 (J.R.H.), the W. M. Keck Foundation (K.B.S.), and a subcontract from the MITRE Corporation (J.R.H.). Postdoctoral and graduate fellowships were provided by the NSF and PEO (H.D.A.), the Gates Foundation (R.D.R.), the NSERC (J.E.H.), and the NCI (S.W.M.). We also acknowledge H. C. Kolb, S. S. Lee, J. Cha, J. Lim, S. Tan, S. Y. Yeo, A. Srivastava, M. Barrientos, E. Johnson Chavarria, A. Stuparu, J. Vielmetter, and C. S. Parker for useful discussions and assistance.
NIH RePORTER
Current address: Department of Bioscience and Biotechnology Konkuk University, Seoul, 143-701 (Korea)
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200900488