Hostname: page-component-78c5997874-fbnjt Total loading time: 0 Render date: 2024-11-08T00:06:45.918Z Has data issue: false hasContentIssue false

A Covalently Linked 10 Nm Gold Immunoprobe

Published online by Cambridge University Press:  02 July 2020

Edmund Gutierrez
Affiliation:
Nanoprobes, Incorporated, Stony Brook, NY11790.
Richard D. Powell
Affiliation:
Nanoprobes, Incorporated, Stony Brook, NY11790.
James F. Hainfeld
Affiliation:
Biology Department, Brookhaven National Laboratory, Upton, NY11973
Peter M. Takvorian
Affiliation:
Biological Sciences Department, Rutgers University, Newark, NJ07102.
Get access

Extract

Chemically functionalized metal cluster compounds have demonstrated important advantages over colloidal gold as biological microscopy labels. They are covalently cross-linked to the targeting biomolecule, and therefore may be conjugated to a wide range of molecules which cannot be labeled with colloidal gold. The 1.4 nm Nanogold® cluster has been conjugated to peptides, lipids and oligonucleotides, some of which have been proposed as elements of novel molecular wires and novel materials. Dissociation of colloidal gold particles from the conjugate probe, a source of error in quantitative immunogold studies, is greatly reduced by covalent cross-linking. Nanogold® is an uncharged molecule, and because its surface is completely coordinated by organic ligands, nonspecific binding is greatly reduced. Nanogold® conjugates also show greatly enhanced penetration into cells and tissue sections. However, gold probes larger than Nanogold® are desirable for improved visualization in specimens with electron-dense regions or staining, or for applications such as double labeling studies with different sized gold labels, or visualizing wider antigen distributions.

Type
Cytochemistry
Copyright
Copyright © Microscopy Society of America

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Gregori, L., et al., J. Biol. Chem., 272 (1997) 58.CrossRefGoogle Scholar
2.Adler-Moore, J., Bone Marrow Transplantation, 14 (1994) S3.Google Scholar
3.Alivisatos, A. P., et al., Nature, 382 (1996) 609.CrossRefGoogle Scholar
4.Behnke, O., et al., Eur. J. Cell Biol., 41 (1986) 326.Google Scholar
5.Hainfeld, J. F., Proc. XIIInt. Cong. Elec. Microsc.(1990) p. 954955.Google Scholar
6.Takizawa, T., and Robinson, J. O., J. Histochem. Cytochem., 43 (1994) 1615.CrossRefGoogle Scholar
7.Slot, J. W., and Geuze, H. J., Eur. J. Cell Biol, 38 (1985) 8.Google Scholar
8.Ths work was partly supported by SBIR grant number R44 GM50048.Google Scholar