Government-Owned Inventions; Availability for Licensing, 9659-9660 [05-3830]

Agencies

• DEPARTMENT OF HEALTH AND HUMAN SERVICES
• National Institutes of Health

[Federal Register Volume 70, Number 38 (Monday, February 28, 2005)]
[Notices]
[Pages 9659-9660]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 05-3830]


-----------------------------------------------------------------------

DEPARTMENT OF HEALTH AND HUMAN SERVICES

National Institutes of Health


Government-Owned Inventions; Availability for Licensing

AGENCY: National Institutes of Health, Public Health Service, DHHS.

ACTION: Notice.

-----------------------------------------------------------------------

SUMMARY: The inventions listed below are owned by an agency of the U.S. 
Government and are available for licensing in the U.S. in accordance 
with 35 U.S.C. 207 to achieve expeditious commercialization of results 
of federally-funded research and development. Foreign patent 
applications are filed on selected inventions to extend market coverage 
for companies and may also be available for licensing.

ADDRESSES: Licensing information and copies of the U.S. patent 
applications listed below may be obtained by writing to the indicated 
licensing contact at the Office of Technology Transfer, National 
Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville, 
Maryland 20852-3804; telephone: 301/496-7057; fax: 301/402-0220. A 
signed Confidential Disclosure Agreement will be required to receive 
copies of the patent applications.

Compositions and Methods for the Treatment of Immune-Related Disease

    F. Xavier Valencia and Peter E. Lipsky (NIAMS), U.S. Provisional 
Application filed 07 Jan 2005 (DHHS Reference No. E-355-2004/0-US-01).
    Licensing Contact: Fatima Sayyid; 301/435-4521; 
sayyidf@mail.nih.gov.
    The ability of the immune system to discriminate between self and 
non-self is controlled by central and peripheral tolerance mechanisms. 
One of the most important ways the immune system controls the outcome 
of such a response is through naturally occurring CD4+CD25+ regulatory 
T cells.
    The present invention relates to compositions and methods for 
treating immune related disease, a method for determining the presence 
of or predisposition to an immune related disease, and a pharmaceutical 
composition for treating an immune related disease in a mammal.
    In addition to licensing, the technology is available for further 
development through collaborative research opportunities with the 
inventors.

Expression Tags for High Yield Soluble Expression of Recombinant 
Proteins

    Deb K. Chatterjee and Dominic Esposito (NCI), U.S. Provisional 
Application No. 60/564,982 filed 26 Apr 2004 (DHHS Reference No. E-103-
2004/0-US-01).
    Licensing Contact: Susan Carson, 301-435-5020; 
carsonsu@mail.nih.gov.
    Production of large quantities of soluble and correctly folded 
proteins is essential for a variety of applications ranging from 
functional analysis and structure determination to clinical trials. E. 
coli is a widely used expression system that offers the advantages of 
ease of handling, cost-effectiveness and the ability to produce 
proteins in high yield. However, the enhanced production obtainable 
with E. coli expression systems is frequently accompanied by problems 
of protein insolubility, production host non-viability and aberrant 
protein folding. Many strategies have been proposed to address these 
problems, in particular the use of fusion vectors that mediate the 
expression of a target gene linked to a peptide signal sequence or to a 
``chaperone'' or ``carrier'' protein that is capable of ``escorting'' 
the fusion protein out of the cytoplasm and into the periplasmic space. 
However, there remains a need for methods that provide soluble proteins 
that are correctly folded and in functional form without unacceptably 
diminishing the yield of recovered protein or requiring complex host 
strains.
    NIH researchers have developed a fusion polynucleotide in which a 
polynucleotide encoding a desired target protein is linked to one or 
more chaperone protein domains (Skp and DsbC) with or without the 
signal sequence. This permits the expressed proteins to be transported 
to the periplasm or to be retained in the cytoplasm respectively and 
these vectors were used to successfully express significant amounts of 
such difficult to express proteins as Hif1a, Folliculin (fol), a 
Folliculin domain (FD), Wnt5a, Endostatin, YopD, IL13 and IFN-Hybrid3. 
These fusion vectors are available for licensing and are useful tools 
for the expression of commercially viable amounts of functional 
proteins of therapeutic and scientific interest.
    In addition to licensing, the technology is available for further 
development through collaborative research with the inventors via a 
Cooperative Research and Development Agreement (CRADA).

Novel Potent Monoamine Oxidase Inhibitors

    Kenneth L. Kirk et al. (NIDDK), U.S. Provisional Application No. 
60/484,710 filed 03 Jul 2003 (DHHS Reference No. E-226-2003/0-US-01); 
PCT Application No. PCT/US04/21505 filed 01 Jul 2004 (DHHS Reference 
No. E-226-2003/0-PCT-02).
    Licensing Contact: Norbert Pontzer; 301/435-5502; 
pontzern@mail.nih.gov.
    Copper- (EC, 1.4.3.6) and flavin-containing amine oxidases (EC, 
1.4.3.4) make up two general classes of the widely distributed 
monoamine oxidases. Reversible and irreversible inhibitors of the 
flavin monoamine oxidases have been developed and investigated for 
treatment of diseases of the CNS such as depression, Parkinson's 
disease and Alzheimer's disease. These researchers have developed 
several new arylethyl and benzyl amine derivatives that incorporate 
both the key cyclopropane ring and fluorine substitution at strategic 
positions. The combined effects of this substitution pattern have led 
to new inhibitors of greatly increased potency and selectivity for all 
classes of monoamine oxidases. Their potent copper amine oxidase 
inhibitors are the best reversible inhibitors known and could provide 
vascular protection in advanced diabetics. Further information on these 
compounds can be found in Yoshida et al., J. Med. Chem. (25 Mar 2004) 
47 (7): 1796-1806, 2004, and Yoshida et al.,

[[Page 9660]]

Bioorg. Med. Chem. (15 May 2004) 12 (10): 2645-2652.

    Dated: February 17, 2005.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 05-3830 Filed 2-25-05; 8:45 am]
BILLING CODE 4140-01-P