Abstract
Macrocyclization of a bioactive peptide with a bifunctional near-infrared fluorescent optical probe gives a compound that retained the receptor binding affinity of the peptide and the photophysical properties of the optical probe. The robust nature of the new compound provides a structural framework for optimizing the activity of bioactive molecules and for monitoring chemical or biological processes in vivo and in vitro by near-infrared optical methods.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Cyclization
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Macromolecular Substances
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry*
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Peptides, Cyclic / chemical synthesis
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Peptides, Cyclic / chemistry*
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Receptors, Somatostatin / chemistry*
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Spectroscopy, Near-Infrared
Substances
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Macromolecular Substances
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Oligopeptides
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Peptides, Cyclic
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Receptors, Somatostatin