Government-Owned Inventions; Availability for Licensing, 9668-9670 [2012-3824]

Agencies

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

[Federal Register Volume 77, Number 33 (Friday, February 17, 2012)]
[Notices]
[Pages 9668-9670]
From the Federal Register Online via the Government Printing 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; 
mccuepat@mail.nih.gov.

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; 
ps193c@nih.gov.
    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 jmconrad@mail.nih.gov.

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; 
tarak@mail.nih.gov.

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; 
vepas@mail.nih.gov.
    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 cdriscoll@mail.nih.gov.

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; 
changke@mail.nih.gov.
    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