Government-Owned Inventions; Availability for Licensing, 3275-3277 [2012-1266]
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Federal Register / Vol. 77, No. 14 / Monday, January 23, 2012 / Notices
functional inhibitory fragment from the
C-terminus of HIV, SHIV or SIV, or an
inhibitory peptide derived from the Nterminus receptor-binding domain of
SIV gp41, HIV–1 gp41, or HIV–2 gp41.
The secreted anti-HIV peptide can also
be a peptide from the allosteric domain
of gp120, an extracellular loop of CCR5,
an anti-CD4 immunoglobulin, a mimetic
of CD4, an alpha-defensin or thetadefensin, a CD38 fragment homologous
to the V3 loop of gp120, polphemusin
II (a CXCR4 antagonist), a RANTES
peptide that binds to CCR5 or an HIV
surface binding peptide such as
cyanovirin.
Potential Commercial Applications:
HIV therapeutics.
Competitive Advantages: Utilizes
naturally occurring commensal bacteria.
Development Stage
• Pre-clinical.
• In vivo data available (animal).
Inventor: Dean H. Hamer (NCI).
Publications
1. Lagenaur LA, et al. Prevention of
vaginal SHIV transmission in macaques
by a live recombinant Lactobacillus.
Mucosal Immunol. 2011 Nov;4(6):648–
657. [PMID 21734653].
2. Rao S, et al. Toward a live
microbial microbicide for HIV:
commensal bacteria secreting an HIV
fusion inhibitor peptide. Proc Natl Acad
Sci U S A. 2005 Aug 23;102(34):11993–
11998. [PMID 16040799].
Intellectual Property
HHS Reference No. E–233–2004/0—
• U.S. Patent Application No. 11/
710,512 filed 26 Feb 2007.
• Various international issued
patents.
Licensing Contact: Michael
Shmilovich, Esq.; (301) 435–5019;
shmilovm@mail.nih.gov.
Dated: January 17, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2012–1264 Filed 1–20–12; 8:45 am]
BILLING CODE 4140–01–P
TKELLEY on DSK3SPTVN1PROD with NOTICES
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
AGENCY:
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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.
SUMMARY:
Thioxothiazolidinone Derivatives—A
Novel Class of Anti Cancer Agents
Description of Technology: The
invention provides for a novel class of
heterocyclic compounds (i.e.
thioxothiazolidinone derivatives) that
exhibit anticancer activity in a unique
mechanism. More specifically, the
compounds of the invention act as
inhibitors of the enzyme human tyrosyl
DNA phosphodiesterase1 (Tdp1), a DNA
repair enzyme involved in
topoisomerase1 (Top1) mediated DNA
damage, such as damage induced by the
Top1 inhibitors and chemotherapeutic
agents, camptothecins. As such, these
compounds can serve as potentiators of
camptothecins. The experimental data
indeed point at a synergistic effect
achieved in a combination therapy of
the thioxothiazolidinone derivatives of
the invention and the established
anticancer agents camptothecins.
Moreover, due to this synergistic effect,
a lower therapeutic dose of the latter
may be needed, resulting in reduced
side effects. In addition, it is possible
that the Tdp1 inhibitors of the invention
may be effective as anti tumor agents on
their own. This is based on the fact that
Tdp1 is involved also in repairing DNA
damage resulting from oxygen radicals,
and the observation that tumors contain
excess free radicals.
Potential Commercial Applications
• Effective cancer therapy in
combination with camptothecins.
• Cancer therapy as standalone anti
cancer agents.
Competitive Advantages: The
compounds of the invention act in
unique mechanism that can enhance the
therapeutic efficacy of the anticancer
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drugs camptothecins, and at the same
time can serve as standalone anticancer
agents.
Development Stage: In vitro data
available.
Inventors: Yves G. Pommier (NCI) et
al.
Publications
1. Marchand C, et al. Identification of
phosphotyrosine mimetic inhibitors of
human tyrosyl-DNA phosphodiesterase
I by a novel AlphaScreen highthroughput assay. Mol Cancer Ther.
2009 Jan;8(1):240–248. [PMID
19139134].
2. Dexheimer TS, et al. Tyrosyl-DNA
phosphodiesterase as a target for
anticancer therapy. Anticancer Agents
Med Chem. 2008 May;8(4):381–389.
[PMID 18473723].
3. Dexheimer TS, et al. 4–Pregnen-21ol-3,20-dione-21-(4bromobenzenesufonate) (NSC 88915)
and related novel steroid derivatives as
tyrosyl-DNA phosphodiesterase (Tdp1)
inhibitors. J Med Chem. 2009 Nov
26;52(22): 7122–7131. [PMID 19883083].
Intellectual Property: HHS Reference
No. E–239–2011/0—U.S. Provisional
Patent Application No. 61/545,308 filed
10 Oct 2011.
Licensing Contact: Uri Reichman,
Ph.D., MBA; (301) 435–4616;
reichmau@mail.nih.gov.
Monospecific and Bispecific Human
Monoclonal Antibodies Targeting IGF–
II
Description of Technology: The type 1
insulin-like growth factor (IGF) receptor
(IGF1R) is over-expressed by many
tumors and mediates proliferation,
motility, and protection from apoptosis.
Agents that inhibit IGF1R expression or
function can potentially block tumor
growth and metastasis. Its major ligands,
IGF–I, and IGF–II are over-expressed by
multiple tumor types. Previous studies
indicate that inhibition of IGF–I, and/or
IGF–II binding to its cognizant receptor
negatively modulates signal
transduction through the IGF pathway
and concomitant cell proliferation and
growth. Therefore, use of humanized or
fully human antibodies against IGFs
represents a valid approach to inhibit
tumor growth. The present invention
discloses two monoclonal antibodies,
designated m610.27 and m630, and a
bispecific monoclonal antibody, m660,
generated by linking domains from
m610.27 and m630. All three antibodies
display high affinities for IGF–I and
IGF–II in the pM to nM range. The
antibodies inhibited signal transduction
mediated by the IGF–1R interaction
with IGF–I and IGF–II and blocked
phosphorylation of IGF–IR and the
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Federal Register / Vol. 77, No. 14 / Monday, January 23, 2012 / Notices
insulin receptor. m610.27 and m630 are
the first pair of human antibodies that
target nonoverlapping epitopes on IGF–
II. All three antibodies in an IgG1 or
IgG1-like format could lead to
irreversible elimination of IGF–II from
circulation making it a viable candidate
for cancer treatment.
Potential Commercial Applications
• Therapeutic for the treatment of
various human diseases associated with
aberrant cell growth and motility such
as breast, prostate, and leukemia
cancers.
• Research reagent to study IGF–I
and/or IGF–II binding and its
association with tumor growth.
Competitive Advantages
• m610.27 and m630 are the first
characterized antibodies that target
nonoverlapping epitopes on IGF–II.
• m660 was generated from two
domains; one each from m610.27 and
m630.
• Small size of the m610.27 and m630
domains prevent overlapping in binding
to IGF–II.
Development Stage
• Pre-clinical.
• In vitro data available.
Inventors: Dimiter S Dimitrov, Weizao
Chen, Yang Feng (NCI).
Intellectual Property: HHS Reference
No. E–212–2011—U.S. Provisional
Application No. 61/548,164 filed 17 Oct
2011.
TKELLEY on DSK3SPTVN1PROD with NOTICES
Related Technologies
• HHS Reference No. E–217–2005/
2—U.S. Patent No. 7,824,681 issued 02
Nov 2010; U.S. Patent Application No.
12/889,345 filed 23 Sep 2010.
• HHS Reference No. E–336–2005/
0—U.S. Patent Application No. 12/
296,328 filed 07 Oct 2008.
• HHS Reference No. E–232–2009/
0—PCT Application No. PCT/US2010/
051784 filed 07 Oct 2010.
• HHS Reference No. E–068–2011/
0—U.S. Provisional Application No. 61/
474,664 filed 12 Apr 2011.
Licensing Contact: Whitney Hastings;
(301) 451–7337; hastingw@mail.nih.gov.
Collaborative Research Opportunity:
The NCI CCR Nanobiology Program is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize this
technology. For collaboration
opportunities, please contact John
Hewes, Ph.D. at hewesj@mail.nih.gov.
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Genetic Interactions That Predict
Attention Deficit Hyperactivity
Disorder Outcome and Severity
Description of Technology:
Genotyping of attention deficit
hyperactivity disorder (ADHD) linked
chromosomal regions containing single
nucleotide polymorphisms (SNPs) was
used by researchers at the National
Human Genome Research Institute
(NHGRI) to discover gene interactions
that increase the risk of developing
ADHD and predict ADHD severity.
NHGRI researchers discovered an
ADHD linked gene interaction between
the latrophilin 3 (LPHN3) gene and a
haplotype on chromosome 11q that
contains the gene coding for the
dopamine receptor D2 (DRD2) and
neural cell adhesion molecule 1
(NCAM1). In a similar invention,
mutations in LPHN3 were shown to
increase the risk of developing ADHD
(HHS E–312–2006, TAB 1504).
Expanding on those findings, this
invention describes an interaction
between LPHN3 and 11q that not only
doubles the risk of developing ADHD,
but also the severity of ADHD.
Furthermore, the LPHN3–11q
interaction correlates with patient
response to therapeutic treatments.
In summary, this invention can be
used to develop biomarkers for
determining susceptibility to and
severity of ADHD, as well as,
developing theranostic assays for
determining prognosis of ADHD
treatments. In addition, signaling
pathways delineated from these genetic
sites can be used to develop better
ADHD therapeutics.
Potential Commercial Applications
• Biomarkers for ADHD susceptibility
and severity.
• Prognostic assays.
• Personalized treatment options.
Competitive Advantages: Improved
prediction of ADHD susceptibility,
severity, and possibly patient response
to treatment.
Development Stage
• Early-stage.
• In vivo data available (human).
Inventors: Maximilian Muenke,
Mauricio Arcos-Burgos, and Maria T.
Acosta (NHGRI).
Publications
1. Jain M, et al. A cooperative
interaction between LPHN3 and 11q
doubles the risk for ADHD. Mol
Psychiatry. 2011 May 24. (Epub ahead
of print) [PMID: 21606926].
2. Arcos-Burgos M and Muenke M.
Toward a better understanding of
ADHD: LPHN3 gene variants and the
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susceptibility to develop ADHD. Atten
Defic Hyperact Disord. 2010
Nov;2(3):139–147. [PMID: 21432600].
Intellectual Property: HHS Reference
No. E–187–2011/0—U.S. Provisional
Application No. 61/505,864 filed on 08
July 2011.
Related Technology: HHS Reference
No. E–312–2006/0—U.S. Patent No.
8,003,406 issued on 23 August 2011.
Licensing Contact: Charlene Sydnor,
Ph.D.; (301) 435–4689;
sydnorc@mail.nih.gov.
Modulating Autophagy as a Treatment
for Lysosomal Storage Diseases
Description of Technology:
Researchers at NIAMS have developed a
technology for treatment of lysosomal
storage diseases by inhibition of
autophagy. Pompe disease is an
example of a genetic lysosomal storage
disease caused by a reduction or
absence of acid alpha-glucosidase
(GAA). Patients with Pompe disease
have a lysosomal buildup of glycogen in
cardiac and skeletal muscle cells and
severe cardiomyopathy and skeletal
muscle myopathy. Treatment of Pompe
disease by GAA enzyme replacement
therapy is quite ineffective for the
skeletal muscle myopathy. Skeletal
muscle resistance to therapy is
associated with increased cellular
buildup of autophagic debris.
Inactivation of autophagy results in
effective GAA replacement therapy and
a reduction in glycogen back to normal
levels. This technology provides a novel
approach for the treatment of Pompe
disease as well as other diseases where
autophagy is a critical contributor to
disease development.
Potential Commercial Applications
• Development of tools for autophagy
suppression and treatment of a variety
of diseases.
• Development of chemical inhibitors
of autophagy.
• Development of animal models to
study lysosomal storage diseases.
Competitive Advantages
• This technology is the first use of
autophagy disablement to reverse an
intracellular pathology.
• More effective than enzyme
replacement therapy alone for the
treatment of the lysosomal storage
disease, Pompe disease.
Development Stage: In vivo data
available (animal).
Inventors: Nina Raben, Cynthia N.
Schreiner, Paul H. Plotz, Shoichi
Takikita, Tao Xie, Rebecca Baum
(NIAMS).
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Federal Register / Vol. 77, No. 14 / Monday, January 23, 2012 / Notices
Publications
1. Raben N, et al. Suppression of
autophagy permits successful enzyme
replacement therapy in a lysosomal
storage disorder—murine Pompe
disease. Autophagy. 2010
Nov;6(8):1078–1089. [PMID 20861693].
2. Raben N, et al. Suppression of
autophagy in skeletal muscle uncovers
the accumulation of ubiquitinated
proteins and their potential role in
muscle damage in Pompe disease. Hum
Mol Genet. 2008 Dec 15;17(24):3897–
3908. [PMID 18782848].
Intellectual Property: HHS Reference
No. E–210–2009/0—PCT Application
No. PCT/US2010/047730 filed 02 Sep
2010.
Licensing Contact: Jaime Greene,
M.S.; (301) 435–5559;
greenejaime@mail.nih.gov.
Collaborative Research Opportunity:
The National Institutes of Health is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize the
technology for disabling autophagy as a
treatment for lysosomal storage diseases.
For collaboration opportunities, please
contact Cecilia Pazman at
pazmance@mail.nih.gov.
Dated: January 17, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2012–1266 Filed 1–20–12; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
TKELLEY on DSK3SPTVN1PROD with NOTICES
Center for Scientific Review; Notice of
Closed Meetings
Pursuant to section 10(d) of the
Federal Advisory Committee Act, as
amended (5 U.S.C. App.), notice is
hereby given of the following meetings.
The meetings will be closed to the
public in accordance with the
provisions set forth in sections
552b(c)(4) and 552b(c)(6), Title 5 U.S.C.,
as amended. The grant applications and
the discussions could disclose
confidential trade secrets or commercial
property such as patentable material,
and personal information concerning
individuals associated with the grant
applications, the disclosure of which
would constitute a clearly unwarranted
invasion of personal privacy.
Name of Committee: Center for Scientific
Review Special Emphasis Panel Member
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Conflict: Risk Prevention and Health
Behavior.
Date: February 14–15, 2012.
Time: 10 a.m. to 6 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Virtual Meeting).
Contact Person: Rebecca Henry, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 3222,
MSC 7808, Bethesda, MD 20892, (301) 435–
1717, henryrr@mail.nih.gov.
Name of Committee: Center for Scientific
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Translational Imaging Applications.
Date: February 15, 2012.
Time: 10 a.m. to 6 p.m.
Agenda: To review and evaluate grant
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Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892.
Contact Person: Antonio Sastre, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 5215,
MSC 7412, Bethesda, MD 20892, (301) 435–
2592, sastrea@csr.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel PAR–11–
044: Indo-US Collaborative Program on LowCost Medical Devices.
Date: February 15–16, 2012.
Time: 11 a.m. to 6 p.m.
Agenda: To review and evaluate grant
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Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Virtual Meeting).
Contact Person: David R Filpula, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 6181,
MSC 7892, Bethesda, MD 20892, (301) 435–
2902, filpuladr@mail.nih.gov.
Name of Committee: Biological Chemistry
and Macromolecular Biophysics Integrated
Review Group; Biochemistry and Biophysics
of Membranes Study Section.
Date: February 16–17, 2012.
Time: 8 a.m. to 5 p.m.
Agenda: To review and evaluate grant
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Place: Hotel Monaco, 700 F Street NW.,
Washington, DC 20001.
Contact Person: Nuria E. Assa-Munt, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 4164,
MSC 7806, Bethesda, MD 20892, (301) 451–
1323, assamunu@csr.nih.gov.
Name of Committee: Emerging
Technologies and Training Neurosciences
Integrated Review Group; Molecular
Neurogenetics Study Section.
Date: February 16–17, 2012.
Time: 8 a.m. to 5 p.m.
Agenda: To review and evaluate grant
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Place: Handlery Union Square Hotel, 351
Geary Street, San Francisco, CA 94102.
Contact Person: Eugene Carstea, Ph.D.,
Scientific Review Officer, Center for
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Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 5194,
MSC 7846, Bethesda, MD 20892, (301) 408–
9756, carsteae@csr.nih.gov.
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Scientific Review Officer, Center for
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Health, 6701 Rockledge Drive, Room 5126,
MSC 7854, Bethesda, MD 20892, (301) 435–
2409, shabestb@csr.nih.gov.
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and Function E Study Section.
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Contact Person: Nitsa Rosenzweig, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 4152,
MSC 7760, Bethesda, MD 20892, (301) 435–
1747, rosenzweign@csr.nih.gov.
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Avenue, Bethesda, MD 20814.
Contact Person: Luis Espinoza, Ph.D.,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 6183,
MSC 7804, Bethesda, MD 20892, (301) 495–
1213, espinozala@mail.nih.gov.
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E:\FR\FM\23JAN1.SGM
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]]>Agencies
[Federal Register Volume 77, Number 14 (Monday, January 23, 2012)]
[Notices]
[Pages 3275-3277]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2012-1266]
-----------------------------------------------------------------------
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.
-----------------------------------------------------------------------
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.
Thioxothiazolidinone Derivatives--A Novel Class of Anti Cancer Agents
Description of Technology: The invention provides for a novel class
of heterocyclic compounds (i.e. thioxothiazolidinone derivatives) that
exhibit anticancer activity in a unique mechanism. More specifically,
the compounds of the invention act as inhibitors of the enzyme human
tyrosyl DNA phosphodiesterase1 (Tdp1), a DNA repair enzyme involved in
topoisomerase1 (Top1) mediated DNA damage, such as damage induced by
the Top1 inhibitors and chemotherapeutic agents, camptothecins. As
such, these compounds can serve as potentiators of camptothecins. The
experimental data indeed point at a synergistic effect achieved in a
combination therapy of the thioxothiazolidinone derivatives of the
invention and the established anticancer agents camptothecins.
Moreover, due to this synergistic effect, a lower therapeutic dose of
the latter may be needed, resulting in reduced side effects. In
addition, it is possible that the Tdp1 inhibitors of the invention may
be effective as anti tumor agents on their own. This is based on the
fact that Tdp1 is involved also in repairing DNA damage resulting from
oxygen radicals, and the observation that tumors contain excess free
radicals.
Potential Commercial Applications
Effective cancer therapy in combination with
camptothecins.
Cancer therapy as standalone anti cancer agents.
Competitive Advantages: The compounds of the invention act in
unique mechanism that can enhance the therapeutic efficacy of the
anticancer drugs camptothecins, and at the same time can serve as
standalone anticancer agents.
Development Stage: In vitro data available.
Inventors: Yves G. Pommier (NCI) et al.
Publications
1. Marchand C, et al. Identification of phosphotyrosine mimetic
inhibitors of human tyrosyl-DNA phosphodiesterase I by a novel
AlphaScreen high-throughput assay. Mol Cancer Ther. 2009 Jan;8(1):240-
248. [PMID 19139134].
2. Dexheimer TS, et al. Tyrosyl-DNA phosphodiesterase as a target
for anticancer therapy. Anticancer Agents Med Chem. 2008 May;8(4):381-
389. [PMID 18473723].
3. Dexheimer TS, et al. 4-Pregnen-21-ol-3,20-dione-21-(4-
bromobenzenesufonate) (NSC 88915) and related novel steroid derivatives
as tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors. J Med Chem. 2009
Nov 26;52(22): 7122-7131. [PMID 19883083].
Intellectual Property: HHS Reference No. E-239-2011/0--U.S.
Provisional Patent Application No. 61/545,308 filed 10 Oct 2011.
Licensing Contact: Uri Reichman, Ph.D., MBA; (301) 435-4616;
reichmau@mail.nih.gov.
Monospecific and Bispecific Human Monoclonal Antibodies Targeting IGF-
II
Description of Technology: The type 1 insulin-like growth factor
(IGF) receptor (IGF1R) is over-expressed by many tumors and mediates
proliferation, motility, and protection from apoptosis. Agents that
inhibit IGF1R expression or function can potentially block tumor growth
and metastasis. Its major ligands, IGF-I, and IGF-II are over-expressed
by multiple tumor types. Previous studies indicate that inhibition of
IGF-I, and/or IGF-II binding to its cognizant receptor negatively
modulates signal transduction through the IGF pathway and concomitant
cell proliferation and growth. Therefore, use of humanized or fully
human antibodies against IGFs represents a valid approach to inhibit
tumor growth. The present invention discloses two monoclonal
antibodies, designated m610.27 and m630, and a bispecific monoclonal
antibody, m660, generated by linking domains from m610.27 and m630. All
three antibodies display high affinities for IGF-I and IGF-II in the pM
to nM range. The antibodies inhibited signal transduction mediated by
the IGF-1R interaction with IGF-I and IGF-II and blocked
phosphorylation of IGF-IR and the
[[Page 3276]]
insulin receptor. m610.27 and m630 are the first pair of human
antibodies that target nonoverlapping epitopes on IGF-II. All three
antibodies in an IgG1 or IgG1-like format could lead to irreversible
elimination of IGF-II from circulation making it a viable candidate for
cancer treatment.
Potential Commercial Applications
Therapeutic for the treatment of various human diseases
associated with aberrant cell growth and motility such as breast,
prostate, and leukemia cancers.
Research reagent to study IGF-I and/or IGF-II binding and
its association with tumor growth.
Competitive Advantages
m610.27 and m630 are the first characterized antibodies
that target nonoverlapping epitopes on IGF-II.
m660 was generated from two domains; one each from m610.27
and m630.
Small size of the m610.27 and m630 domains prevent
overlapping in binding to IGF-II.
Development Stage
Pre-clinical.
In vitro data available.
Inventors: Dimiter S Dimitrov, Weizao Chen, Yang Feng (NCI).
Intellectual Property: HHS Reference No. E-212-2011--U.S.
Provisional Application No. 61/548,164 filed 17 Oct 2011.
Related Technologies
HHS Reference No. E-217-2005/2--U.S. Patent No. 7,824,681
issued 02 Nov 2010; U.S. Patent Application No. 12/889,345 filed 23 Sep
2010.
HHS Reference No. E-336-2005/0--U.S. Patent Application
No. 12/296,328 filed 07 Oct 2008.
HHS Reference No. E-232-2009/0--PCT Application No. PCT/
US2010/051784 filed 07 Oct 2010.
HHS Reference No. E-068-2011/0--U.S. Provisional
Application No. 61/474,664 filed 12 Apr 2011.
Licensing Contact: Whitney Hastings; (301) 451-7337;
hastingw@mail.nih.gov.
Collaborative Research Opportunity: The NCI CCR Nanobiology Program
is seeking statements of capability or interest from parties interested
in collaborative research to further develop, evaluate or commercialize
this technology. For collaboration opportunities, please contact John
Hewes, Ph.D. at hewesj@mail.nih.gov.
Genetic Interactions That Predict Attention Deficit Hyperactivity
Disorder Outcome and Severity
Description of Technology: Genotyping of attention deficit
hyperactivity disorder (ADHD) linked chromosomal regions containing
single nucleotide polymorphisms (SNPs) was used by researchers at the
National Human Genome Research Institute (NHGRI) to discover gene
interactions that increase the risk of developing ADHD and predict ADHD
severity.
NHGRI researchers discovered an ADHD linked gene interaction
between the latrophilin 3 (LPHN3) gene and a haplotype on chromosome
11q that contains the gene coding for the dopamine receptor D2 (DRD2)
and neural cell adhesion molecule 1 (NCAM1). In a similar invention,
mutations in LPHN3 were shown to increase the risk of developing ADHD
(HHS E-312-2006, TAB 1504). Expanding on those findings, this invention
describes an interaction between LPHN3 and 11q that not only doubles
the risk of developing ADHD, but also the severity of ADHD.
Furthermore, the LPHN3-11q interaction correlates with patient response
to therapeutic treatments.
In summary, this invention can be used to develop biomarkers for
determining susceptibility to and severity of ADHD, as well as,
developing theranostic assays for determining prognosis of ADHD
treatments. In addition, signaling pathways delineated from these
genetic sites can be used to develop better ADHD therapeutics.
Potential Commercial Applications
Biomarkers for ADHD susceptibility and severity.
Prognostic assays.
Personalized treatment options.
Competitive Advantages: Improved prediction of ADHD susceptibility,
severity, and possibly patient response to treatment.
Development Stage
Early-stage.
In vivo data available (human).
Inventors: Maximilian Muenke, Mauricio Arcos-Burgos, and Maria T.
Acosta (NHGRI).
Publications
1. Jain M, et al. A cooperative interaction between LPHN3 and 11q
doubles the risk for ADHD. Mol Psychiatry. 2011 May 24. (Epub ahead of
print) [PMID: 21606926].
2. Arcos-Burgos M and Muenke M. Toward a better understanding of
ADHD: LPHN3 gene variants and the susceptibility to develop ADHD. Atten
Defic Hyperact Disord. 2010 Nov;2(3):139-147. [PMID: 21432600].
Intellectual Property: HHS Reference No. E-187-2011/0--U.S.
Provisional Application No. 61/505,864 filed on 08 July 2011.
Related Technology: HHS Reference No. E-312-2006/0--U.S. Patent No.
8,003,406 issued on 23 August 2011.
Licensing Contact: Charlene Sydnor, Ph.D.; (301) 435-4689;
sydnorc@mail.nih.gov.
Modulating Autophagy as a Treatment for Lysosomal Storage Diseases
Description of Technology: Researchers at NIAMS have developed a
technology for treatment of lysosomal storage diseases by inhibition of
autophagy. Pompe disease is an example of a genetic lysosomal storage
disease caused by a reduction or absence of acid alpha-glucosidase
(GAA). Patients with Pompe disease have a lysosomal buildup of glycogen
in cardiac and skeletal muscle cells and severe cardiomyopathy and
skeletal muscle myopathy. Treatment of Pompe disease by GAA enzyme
replacement therapy is quite ineffective for the skeletal muscle
myopathy. Skeletal muscle resistance to therapy is associated with
increased cellular buildup of autophagic debris. Inactivation of
autophagy results in effective GAA replacement therapy and a reduction
in glycogen back to normal levels. This technology provides a novel
approach for the treatment of Pompe disease as well as other diseases
where autophagy is a critical contributor to disease development.
Potential Commercial Applications
Development of tools for autophagy suppression and
treatment of a variety of diseases.
Development of chemical inhibitors of autophagy.
Development of animal models to study lysosomal storage
diseases.
Competitive Advantages
This technology is the first use of autophagy disablement
to reverse an intracellular pathology.
More effective than enzyme replacement therapy alone for
the treatment of the lysosomal storage disease, Pompe disease.
Development Stage: In vivo data available (animal).
Inventors: Nina Raben, Cynthia N. Schreiner, Paul H. Plotz, Shoichi
Takikita, Tao Xie, Rebecca Baum (NIAMS).
[[Page 3277]]
Publications
1. Raben N, et al. Suppression of autophagy permits successful
enzyme replacement therapy in a lysosomal storage disorder--murine
Pompe disease. Autophagy. 2010 Nov;6(8):1078-1089. [PMID 20861693].
2. Raben N, et al. Suppression of autophagy in skeletal muscle
uncovers the accumulation of ubiquitinated proteins and their potential
role in muscle damage in Pompe disease. Hum Mol Genet. 2008 Dec
15;17(24):3897-3908. [PMID 18782848].
Intellectual Property: HHS Reference No. E-210-2009/0--PCT
Application No. PCT/US2010/047730 filed 02 Sep 2010.
Licensing Contact: Jaime Greene, M.S.; (301) 435-5559;
greenejaime@mail.nih.gov.
Collaborative Research Opportunity: The National Institutes of
Health is seeking statements of capability or interest from parties
interested in collaborative research to further develop, evaluate or
commercialize the technology for disabling autophagy as a treatment for
lysosomal storage diseases. For collaboration opportunities, please
contact Cecilia Pazman at pazmance@mail.nih.gov.
Dated: January 17, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2012-1266 Filed 1-20-12; 8:45 am]
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