[Federal Register Volume 77, Number 33 (Friday, February 17, 2012)]
[Notices]
[Pages 9668-9670]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 2012-3824]
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DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions; Availability for Licensing
AGENCY: National Institutes of Health, Public Health Service, HHS.
ACTION: Notice.
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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.
Selective Inhibitors of Polo-Like Kinase 1 (PLK1) Polo-Box Domains as
Potential Anticancer Agents
Description of Technology: PLK1 is a regulator of cell growth that
represents a new target for anticancer therapeutic development. High
expression of PLK1 has been associated with several types of cancer
(e.g., breast cancer, prostate cancer, ovarian cancer, non-small cell
lung carcinoma). Inhibiting PLK1 could be an effective treatment for
cancer patients without significant side-effects. Available for
licensing are synthetic peptides with the ability to bind to polo-like
kinase 1 (PLK1) polo-box domains (PBDs) with selectivity and nanomolar
affinity and induce apoptosis in cancer cells. By inhibiting the
functions of PLK1, these peptides could serve as potential anti-cancer
therapies. This technology is related to and an extension of HHS
technology reference E-181-2009.
Potential Commercial Applications:
New anticancer therapies that specifically target PLK1.
Platform for the development of further improved PLK1
inhibitors.
Competitive Advantages:
High PBD binding affinity.
High binding selectivity.
Development Stage: Early-stage.
Inventors: Terrence R. Burke, Jr. (NCI), et al.
Publications:
1. Liu F, et al. Serendipitous alkylation of a Plk1 ligand uncovers
a new binding channel. Nat Chem Biol. 2011 Jul 17;7(9):595-601. [PMID
21765407]
2. Qian W, et al. Investigation of unanticipated alkylation at the
N(pi) position of a histidyl residue under Mitsunobu conditions and
synthesis of orthogonally protected histidine analogues. J Org Chem.
2011 Nov 4;76(21):8885-8890. [PMID 21950469]
Intellectual Property: HHS Reference No. E-053-2012/0--U.S.
Provisional Application No. 61/588,470 filed 19 Jan 2012.
Related Technology: HHS Reference No. E-181-2009/3--U.S.
Provisional Application No. 61/474,621 filed 12 Apr 2011.
Licensing Contact: Patrick McCue, Ph.D.; 301-435-5560;
[email protected].
Influenza Vaccine
Description of Technology: It has been shown that the fusion
peptide, a sequence comprised of fourteen amino acids at the N-terminal
of the influenza hemagglutinin 2 protein is conserved among A and B
influenza viruses. Monoclonal antibodies against this peptide are
capable of binding all influenza virus HA proteins and inhibit viral
growth by impeding the fusion process between the virus and the target
cell. This application claims immunogenic conjugates comprising the
fusion peptide region linked to a carrier protein. In preclinical
studies, these conjugates were immunogenic and induced booster
responses. The induced antibodies bound to the recombinant HA protein.
This methodology of linking the highly conserved fusion peptide region
to a carrier protein can broaden the protective immune response to
include influenza A and B virus strains. This would eliminate the need
for annual influenza vaccination.
Potential Commercial Applications:
Influenza vaccines
Influenza diagnostics
Research tools
Competitive Advantages:
Universal influenza vaccine
Efficient manufacturing process
May eliminate need for yearly influenza vaccination
Development Stage:
Pre-clinical
In vitro data available
In vivo data available (animal)
Inventors: Joanna Kubler-Kielb, Jerry M. Keith, Rachel Schneerson
(NICHD).
Intellectual Property: HHS Reference No. E-271-2011/0--U.S.
Provisional Application No. 61/541,942 filed 30 Sep 2011.
Licensing Contact: Peter A. Soukas, J.D.; 301-435-4646;
[email protected].
Collaborative Research Opportunity: The NICHD is seeking statements
of capability or interest from parties interested in collaborative
research to further develop, evaluate or commercialize conjugate
influenza vaccines comprising fusion peptide region. For collaboration
opportunities, please contact Joseph Conrad, Ph.D., J.D. at 301-435-
3107 or [email protected].
ACSF3-Based Diagnostics and Therapeutics for Combined Malonic and
Methylmalonic Aciduria (CMAMMA) and Other Metabolic Disorders
Description of Technology: Combined malonic and methylmalonic
aciduria (CMAMMA) is a metabolic disorder in which malonic acid and
methylmalonic acid, key intermediates in fatty acid metabolism,
accumulate in the blood and urine. This disorder is often undetected
until symptoms manifest, which can include developmental delays and a
failure to thrive in children, and psychiatric and neurological
disorders in adults. Once thought to be a very rare disease,
[[Page 9669]]
CMAMMA is now thought to be one of the most common forms of
methylmalonic acidemia, and perhaps one of the most common inborn
errors of metabolism, with a predicted incidence of one in 30,000.
Investigators at the National Human Genome Research Institute
(NHGRI) have identified the genetic cause of CMAMMA, an enzyme encoded
by the ACSF3 (Acyl-CoA Synthetase Family Member 3) gene. This enzyme is
located in the mitochondrion, and appears to be a methylmalonyl-CoA and
malonyl-CoA synthetase, which catalyzes the first step of intra-
mitochondrial fatty acid synthesis. As such, this discovery may not
only be critical for the development of diagnostic tools and treatments
for CMAMMA, but also holds promise for the treatment of other related
metabolic disorders.
Potential Commercial Applications:
Diagnosis of CMAMMA or other metabolic diseases.
Therapies for CMAMMA or other metabolic diseases, such as
lipoic acid administration, gene therapy or enzyme replacement therapy.
Competitive Advantages:
Mutation of ACSF3 has been shown to be the genetic cause
of CMAMMA, and there are no existing methods to diagnose this disorder.
Therapies based on ACSF3 may be applicable to a variety of
metabolic disorders.
Development Stage:
In vivo data available (animal).
In vivo data available (human).
Inventors: Charles P. Venditti, Leslie G. Biesecker, Jennifer L.
Sloan, Jennifer J. Johnston, Eirini Manoli, Randy J. Chandler (all of
NHGRI).
Publication: Sloan JL, et al. Exome sequencing identifies ACSF3 as
a cause of combined malonic and methylmalonic aciduria. Nat Genet. 2011
Aug 14;43(9):883-886. [PMID 21841779]
Intellectual Property: HHS Reference No. E-209-2011/0--U.S.
Provisional Application No. 61/504,030 filed 01 Jul 2011.
Licensing Contact: Tara L. Kirby, Ph.D.; 301-435-4426;
[email protected].
Antagonists of the Hedgehog Pathway as Therapeutics for the Treatment
of Heterotopic Ossification, Vascular Calcification, and Pathologic
Mineralization
Description of Technology: Heterotopic ossification (HO) results
from osteoid formation of mature lamellar bone in soft tissue sites
outside the skeletal periosteum (skeletal system), most commonly around
proximal limb joints. HO can also be caused by genetic diseases such as
progressive osseous heteroplasia (POH) and fibrodysplasia ossificans
progressiva (FOP). Currently, all forms of HO lack adequate treatments
and definite cure. Vascular calcification is a complex process that
involves biomineralization and resembles osteogenesis. It is
exacerbated during such conditions as diabetes, osteoporosis,
menopause, hypertension, metabolic syndrome, chronic kidney disease,
and end stage renal disease. In the present technology, the inventors
describe novel methods for preventing or treating HO and vascular
calcification using one or more antagonists of the Hedgehog pathway.
The inventors, using both in vitro (limb culture experiments) and in
vivo studies using Prx1-cre; Gsf/f mice model discovered that the
antagonists of the Hedgehog pathway prevent formation of HO. The
inventors also observed that Prx1-cre; Gsf/f mice developed
calcification or mineralization around their blood vessels, and
treatment with Hedgehog antagonists reduced mineralization throughout
the body of these mice, including regions around the blood vessels, as
observed by mineral staining. The antagonists that can be used to
develop effective therapeutics include zerumbone epoxide, arcyriaflavin
C, 5,6-dihyroxyarcyriaflavin A, physalin F, physalin B, arsenic
trioxide (ATO), sodium arsenite, etc.
Potential Commercial Applications: Development of therapeutics for
heterotopic ossification, vascular calcification, and pathologic
mineralization.
Competitive Advantages: Several clinically tested and FDA-approved
Hedgehog antagonists are currently available and these compounds will
expedite the commercial development of this technology.
Development Stage:
Early-stage.
Pre-clinical.
In vitro data available.
In vivo data available (animal).
Inventors: Yingzi Yang and Jean Regard (NHGRI).
Intellectual Property: HHS Reference No. E-116-2011/0--U.S.
Provisional Application No. 61/504,041 filed 01 Jul 2011.
Licensing Contact: Suryanarayana (Sury) Vepa, Ph.D.; 301-435-5020;
[email protected].
Collaborative Research Opportunity: The National Human Genome
Research Institute (NHGRI) is seeking statements of capability or
interest from parties interested in collaborative research to further
develop, evaluate or commercialize antagonists of the Hedgehog pathway
for treatment of ossification and calcification disorders. For
collaboration opportunities, please contact Claire T. Driscoll at 301-
594-2235 or [email protected].
A Novel Treatment for Malarial Infections
Description of Technology: The inventions described herein are
antimalarial small molecule inhibitors of the plasmodial surface anion
channel (PSAC), an essential nutrient acquisition ion channel expressed
on human erythrocytes infected with malaria parasites. These inhibitors
were discovered by high-throughput screening of chemical libraries and
analysis of their ability to kill malaria parasites in culture. Two
separate classes of inhibitors were found to work synergistically in
combination against PSAC and killed malaria cultures at markedly lower
concentrations than separately. These inhibitors have high affinity and
specificity for PSAC and have acceptable cytotoxicity profiles.
Preliminary in vivo testing of these compounds in a mouse malaria model
is currently ongoing.
Potential Commercial Applications: Treatment of malarial
infections.
Competitive Advantages:
Novel drug treatment for malarial infections.
Synergistic effect of these compounds on PSAC.
Development Stage:
In vitro data available.
In vivo data available (animal).
Inventor: Sanjay A. Desai (NIAID).
Publications:
1. Kang M, et al. Malaria parasites are rapidly killed by
dantrolene derivatives specific for the plasmodial surface anion
channel. Mol. Pharmacol. 2005 Jul;68(1):34-40. [PMID 15843600]
2. Desai SA, et al. A voltage-dependent channel involved in
nutrient uptake by red blood cells infected with the malaria parasite.
Nature. 2000 Aug 31;406(6799):1001-1005. [PMID 10984055]
Patent Status: HHS Reference No. E-202-2008/0--U.S. Patent
Application No. 13/055,104 filed 20 Jan 2011; various international
patent applications.
Licensing Contact: Kevin W. Chang, Ph.D.; 301-435-5018;
[email protected].
Collaborative Research Opportunity: The NIAID Office of Technology
Development is seeking statements of capability or interest from
parties interested in collaborative research to further develop,
evaluate, or commercialize antimalarial drugs that
[[Page 9670]]
target PSAC or other parasite-specific transporters. For collaboration
opportunities, please contact Dana Hsu at 301-496-2644.
Dated: February 13, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2012-3824 Filed 2-16-12; 8:45 am]
BILLING CODE 4140-01-P