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Peptides Linked to Nanogold® Maintain Biologic Activity

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July 10, 1996

July 10, 1996: Several reports have now appeared in the literature describing the covalent attachment of Nanogold® to peptides and their use to track peptide binding both in tissues (using light microscopy) and to individual molecules (using electron microscopy). Retention of activity was demonstrated by Western blots, polyacrylamide gel electophoresis, and competitive binding studies with unlabeled peptide.

Read about these three studies using Nanogold labeling for peptides:

[Micrograph] (77k)

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30 micrometer cryostat section of rat spinal cord labeled with Nanogold- Substance P (SP is an 11 amino acid peptide) showing binding sites of this bioactive peptide. m=motoneurons, x=lamina, I+II=lamina I and II. Silver enhanced; full image width 5 microns.

Courtesey of G. Segond von Banchet and B. Heppelmann, Physiologisches Institut der Universität Würzburg, Würzburg, Germany.


How Nanogold-Peptide Probes Are Made

Nanogold® is a small (1.4 nm) gold cluster with an organic shell and a monofunctonal reactive arm, either a maleimide (which reacts with thiols) or a sulfo-N- hydroxysuccinimide ester (which reacts with amines).

Covalent linking of the Nanogold to peptides may be achieved by reacting with the alpha-NH2 group, a lysine, a terminal cysteine that is added, or an existing cysteine.

[Nanogold conjugation diagram] (4k)

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