Abstract
Peptide aptamers are small combinatorial proteins that are selected to bind to specific sites on their target molecules. Peptide aptamers consist of short, 5-20 amino acid residues long sequences, typically embedded as a loop within a stable protein scaffold. Various peptide aptamer scaffolds and in vitro and in vivo selection techniques are reviewed with emphasis on specific biomedical, bioimaging, and bioanalytical applications.
Keywords: Affibodies, Affilins, Anticalins, Armadillo repeat, Atrimers, Avimers, Cell display, Combinatorial libraries, Darpins, Directed evolution, DNA display, Fynomers, Knottins, Kunitz domain, Monobodies, mRNA display, OBodies, Phage display, Peptide aptamers, Protein scaffold, Ribosome display, Thioredoxin, Yeast two hybrid.
Graphical Abstract
Current Topics in Medicinal Chemistry
Title:Peptide Aptamers: Development and Applications
Volume: 15 Issue: 12
Author(s): Sergey Reverdatto, David S. Burz and Alexander Shekhtman
Affiliation:
Keywords: Affibodies, Affilins, Anticalins, Armadillo repeat, Atrimers, Avimers, Cell display, Combinatorial libraries, Darpins, Directed evolution, DNA display, Fynomers, Knottins, Kunitz domain, Monobodies, mRNA display, OBodies, Phage display, Peptide aptamers, Protein scaffold, Ribosome display, Thioredoxin, Yeast two hybrid.
Abstract: Peptide aptamers are small combinatorial proteins that are selected to bind to specific sites on their target molecules. Peptide aptamers consist of short, 5-20 amino acid residues long sequences, typically embedded as a loop within a stable protein scaffold. Various peptide aptamer scaffolds and in vitro and in vivo selection techniques are reviewed with emphasis on specific biomedical, bioimaging, and bioanalytical applications.
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Cite this article as:
Reverdatto Sergey, Burz S. David and Shekhtman Alexander, Peptide Aptamers: Development and Applications, Current Topics in Medicinal Chemistry 2015; 15 (12) . https://dx.doi.org/10.2174/1568026615666150413153143
DOI https://dx.doi.org/10.2174/1568026615666150413153143 |
Print ISSN 1568-0266 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4294 |
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