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Contents: News Stories, 1997


September 8, 1997

NIGMS awards "Fast-Track" SBIR grant to Nanoprobes to develop Fluorescent and Large Metal Cluster Combination Probes

The National Institute of General Medical Sciences (NIH) has awarded a new SBIR grant to Nanoprobes, Incorporated (Stony Brook, NY) of $ 99,988 for six months. Entitled "Fluorescent and Large Metal Cluster Combination Probes," the grant will support the synthesis and evaluation of molecular labels and targeted probes which combine fluorophores with large metal cluster complexes and chemically functionalized nanoparticles. These will augment our recently developed FluoroNanogold line with new approaches to simultaneous labeling with fluorophores and gold cluster probes. These include the use of gold labeling in conjunction with geen fluorescent protein expression, and the formulation of new labels as reagents with which researchers will be able to site-specifically label a wide variety of biomolecules with both a fluorophore and a heavy atom cluster. This will enable the preparation of a wide range of novel probes and the development of new approaches to biomedical imaging. Detailed investigations are also planned into the energy transfer interactions of fluorescent groups with metal nanoparticles. Insights gained from this work will be used to develop more effective probes, which will provide a new of molecular tools for elucidating the molecular processes ocurring in cells and tissues.

[improved combination probe] (33k)

Configurations for an improved combined fluorescence / EM immunoprobe.

This is the first SBIR grant tobe awarded by NIGMS under the "Fast-Track" pilot program, in which the Phase I and Phase II proposals are reviewed concurrently. Synthesis of the new cluster reagents will be conducted by Dr. Richard D. Powell with Dr. Edmund Gutierrez, Dr. Vishwas N. Joshi, Carol M. R. Halsey and Dr. James F. Hainfeld. Dr. David L. Spector (Cold Spring Harbor Laboratory, NY), Dr. Andrew Belmont (University of Illinois at Urbana-Champaign, IL) will use investigate the structure and function of nuclear proteins using labeled antibodies and small-molecules probes, and Dr. Dick Tuft (Biomedical Imaging group) and Dr. Roger Craig (Cell Biology Department) of the University of Massachusetts Medical Center will use the new probes to correlate their studies of a number of cellular processes at the light and electron microscope levels. The grant also includes a subcontract to the State University of New York at Stony Brook, NY.

For more information, contact:

Richard D. Powell, Ph. D.
Research Director
Nanoprobes, Incorporated
25 East Loop Road, Suite 113
Stony Brook, NY 11790-3350

Telephone: (516) 444-8815
Fax: (516) 444-8816
E-mail [email protected]
WWW: www.nanoprobes.com

contents


September 5, 1997

New FluoroNanogold Papers: Preparation and Applications

Two seminal papers have been published in the May and July 1997 issues of the Journal of Histochemistry and Cytochemistry describing the nature and applications of FluoroNanogold. Dr. John Robinson and Dr. Dale Vandré of Ohio State University used fluorescein and Nanogold®-conjugated anti-rabbit Fab' to label leukocyte microtubules, which they then observed using fluorescence and light microscopy, in a variety of imaging modes, and electron microscopy. The fluorescence signal was preserved even after brief (1-2 minutes) silver enhancement, and the labeling was found to be comparable with either fluorescein or Nanogold® labeling used alone (Robinson, J. M., and Vandré, D. D. Efficient immunocytochemical labeling of leukocyte microtubules with FluoroNanogold: An important tool for correlative microscopy. J. Histochem. Cytochem., 45, 631-642 (1997)).

More details and micrographs

In our own paper (Powell, R. D.; Halsey, Carol M. R.; Spector, D. L.; Kaurin, S. L.; McCann, J., and Hainfeld, J. F.: A covalent fluorescent-gold immunoprobe: "simultaneous" detection of a pre-mRNA splicing factor by light and electron microscopy. J. Histochem. Cytochem., 45, 947-956 (1997)), we describe the preparation and properties of FluoroNanogold. The new probe was then used to label a pre-mRNA splicing factor, SC35, in the HeLa cell nucleus. Dr. David L. Spector of Cold Spring Harbor Laboratory (Cold Spring Harbor, NY) found that the new probes gave fluorescence intensities comparable to commercially available FITC conjugates, and results with gold labeling were comparable to those found with the non-fluorescent Nanogold® probes, and the dense labeling of sites within the nucleus shows that the new probe has the same high cell and nuclear penetration found with Nanogold®.

For more information, contact:

Richard D. Powell, Ph. D.
Research Director
Nanoprobes, Incorporated
25 East Loop Road, Suite 113
Stony Brook, NY 11790-3350

Telephone: (516) 444-8815
Fax: (516) 444-8816
E-mail [email protected]
WWW: www.nanoprobes.com

Link to Micrographs [28k]

Link to EM [31k]

Fluorescence and electron micrographs of labeled SC35 in HeLa cell nucleus. Click on image for link to larger view and complete details (link opens in a new window).

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April 24, 1997

Undecagold and Tetrairidium Membrane Protein Derivatization: NIGMS grants Phase I SBIR to Nanoprobes

[beef bc1 crystals] (33k)

A: Crystals of beef cytochrome reductase grown by sitting drop vapor diffusion, with PEG as precipitant. Crystals are hexagonal bipyramids in the space group P61222 (or P65222).

(Courtesey of Dr. Edward A. Berry, Lawrence Berkely Laboratory)

The National Institute of General Medical Sciences (NIH) has issued a Phase I SBIR grant to Nanoprobes, Incorporated (Stony Brook, NY) of $ 96,385 for six months. Entitled "Heavy Atom Clusters for Membrane Protein Derivatization," the grant will support the synthesis and use of tetrairidium and undecagold cluster complexes for derivatization of membrane proteins for X-ray crystallographic structure determination. Membrane proteins perform key functions in many cellular processes, and their structural biology is of intense interest. However, because they include both hydrophobic and hydrophilic domains which must be differently solvated,both crystallization and crystal structure determination are difficult. Derivatization with heavy atom compounds at unique lattice sites is frequently used to obtain phase information and enable X-ray structure solution of proteins. In this project, cluster compounds will be engineered for derivatization of membrane proteins by using novel ligands to confer hydrophobicity and to introduce partial, asymmetric hydrophilicity: thus the new reagents will be preferentially absorbed and oriented within the hydrophobic (membrane-associated) domains of the proteins. The clusters will be targeted either by reactivity towards unique amino acid residues, or by conjugation to small molecule inhibitors which are bound at active sites. New reagents developed during this project may contribute substantially to our understanding of the structure and role of membrane proteins in biology and their significance for health.

Synthesis of the new cluster reagents will be conducted byDr. Richard D. Powell with Dr. Vishwas N. Joshi, Dr. Frederic Furuya, Carol M. R. Halsey and Dr. James F. Hainfeld. Dr. Edward Berry of the Structural Biology Division at the Lawrence Berkeley Laboratory will use the new reagents in structural studies of the cytochrome bc1 complex. The grant also includes a subcontract to the State University of New York at Stony Brook, NY.

For more information, contact:

Richard D. Powell, Ph. D.
Research Director
Nanoprobes, Incorporated
25 East Loop Road, Suite 113
Stony Brook, NY 11790-3350

Telephone: (516) 444-8815
Fax: (516) 444-8816
E-mail [email protected]
WWW: www.nanoprobes.com

contents


 

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