Federal Register / Vol. 66, No. 103 / Tuesday, May 29, 2001 / Notices 29155

epithelial cells and blocked adherence

of P. aeruginosa on epithelial cells.

When the chimeric protein was injected

into rabbits, the rabbits produced

antibodies that blocked bacterial

adherence and neutralized the cell

killing activity of native exotoxin A.

A Plasmid for Expression of a More

Soluble Form of HIV Integrase Protein

in E. coli

Robert Craigie (NIDDK)

DHHS Reference No. E–110–01/0

Licensing Contact: Sally Hu; 301/496–

7056 ext. 265; e-mail: hus@od.nih.gov

The invention describes a plasmid

that provides a convenient method for

producing large quantities of integrase

protein. This integrase protein is more

soluble because amino acid residue

Phe185 is changed to Lsy. This change

does not affect the in vitro activity of the

protein, but the improved solubility

facilitates large-scale purification and

handling. Since HIV integrase is a

candidate target for antiviral drugs and

an assay system or a source of HIV

integrase is required to identify lead

compounds, this invention could be

very useful for an efficient means of

producing integrase protein on a large

scale. The integrase protein could be

used in screening for integrase

inhibitors that could be developed as

anti-HIV drugs. This invention is

available for licensing through a

Biological Materials License, as no

patent application exists.

Benzoylalkylindolepyridinium

Compounds and Pharmaceutical

Compositions Comprising Such

Compounds

William G. Rice, Mingjun Huang, Robert

W. Buckheit, Jr., David G, Covell,

Grzegorz Czerwinski, Christopher

Michejda, and Vadim Makarov (NCI)

DHHS Reference Nos. E–278–98/0 and

E–278–98/1, filed Dec 18, 2000

Licensing Contact: Sally Hu; 301/496–

7056 ext. 265; e-mail: hus@od.nih.gov

The present invention provides novel

antiviral compounds active against HIV.

These compounds, referred to as

benzoylalkylindolepyridinium

compounds (BAIPs) are effective against

HIV isolates that have developed

mutations rendering conventional drugs

ineffective. BAIPs apparently do not

require intracellular phosphorylation

nor bind to the reverse transcriptase

(RT) active site, which distinguishes

their mechanism of action from the

dideoxynucleoside (ddN) and acyclic

nucleoside phosphonate (ANP)

nucleoside analog drugs. ddN and ANP

have proven clinically effective against

limiting human immunodeficiency

virus (HIV) infection, but resistance

rapidly emerges due to mutations in and

around the RT active site. The BAIPs

also may be distinguished from nonnucleoside reverse transcriptase

inhibitors (NNRTIs), in part because the

BAIPs bind to a different site on the RT

enzyme. The usage of NNRTIs is limited

by the rapid emergence of resistant

strains also. Moreover, unlike the

NNRTIs, BAIPs of the present invention

have been shown to be effective against

HIV–1, HIV–2 and simian

immunodeficiency virus (SIV)

proliferation. Thus, BAIPs are broadly

antiviral, non-nucleoside reverse

transcriptase inhibitors (BANNRTIs).

This abstract modifies an abstract for

this technology published in the

Federal Register on Tuesday, February

13, 2001 (66 FR 10027).

Dated: May 17, 2001.

Jack Spiegel,

Director, Division of Technology Development

and Transfer, Office of Technology Transfer,

National Institutes of Health.

[FR Doc. 01–13345 Filed 5–25–01; 8:45 am]

BILLING CODE 4140–01–P

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 agencies 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.

Combined Inhibition of

Phosphodiesterase-4 (PDE–4) and

Phosphodiesterase-3 (PDF–3) as a

Therapy for Th1 Mediated

Autoimmune Diseases

Dr. Bibiana Bielekova et al. (NINDS)

DHHS Reference No. E–077–00/0, filed

Dec 22 2000

Licensing Contact: Marlene Shinn; 301/

496–7056 ext. 285; e-mail:

shinnm@od.nih.gov

Hyperactive Th1-mediated immune

responses are thought to be involved in

the pathogenesis of many autoimmune

diseases, including rheumatoid arthritis,

diabetes, inflammatory bowel disease,

vitiligo, and multiple sclerosis among

others. Immune cells are known to

produce primarily two classes of

phosphodiesterases (PDE), the PDE4 and

the PDE3 classes. Inhibitors of these

PDEs have been shown to down-regulate

the expression or production of Th1

cytokines and have either no effect or

augment the production of Th2

cytokines, therefore making them good

candidates for the treatment of Th1-

mediated autoimmune diseases.

The NIH announces a new technology

wherein PDE–4 and PDE–3 inhibitors

are used in combination and a

synergistic enhancement of therapeutic

activity is achieved. This results in a

more potent immunomodulatory effect

on the immune cells and could lead to

the administration of lower dose rate of

the inhibitors. This new form of

treatment will alleviate side effects

through the use of a lower dose rate for

each and will make for a more effective

therapy.

Determination of AM-Binding Proteins

and the Association of Adrenomedullin

(AM) Therewith

F. Cuttitta et al. (NCI)

DHHS Reference No. E–256–99/1 filed,

Sep 08 2000 (Note: This invention is

related to E–206–95/3, filed Aug 18

1996, the disclosure of which is

incorporated herein.)

Licensing Contact: Matthew Kiser; 301/

496–7056 ext. 224; e-mail:

kiserm@od.nih.gov

The present invention provides

methods for the isolation, identification,

and purification of adrenomedullin

(AM)-binding proteins. Methods for

utilizing the purified AM-binding

proteins, or functional portions thereof,

to diagnose, treat, and monitor AMrelated diseases are described. A second

aspect of this technology discloses the

identification and isolation of a novel

complex between AM and a specific

AM-binding protein 1 (AMBP–1),

designated factor H (fH). The

identification of small molecule

29156 Federal Register / Vol. 66, No. 103 / Tuesday, May 29, 2001 / Notices

antagonist, which down-regulate the

function of AM, factor H, and the AM/

fH complex has been achieved.

Collectively, the invention provides

methods for treating conditions such as

cancer or diabetes, via antibodies and

small molecule antagonists.

Adrenomedullin (AM) is expressed in

human cancer cell lines of diverse

origin and functions as a universal

autocrine growth factor, driving

neoplastic proliferation. Experimental

models for use in identifying the role of

AM in pancreatic physiology have been

validated and are available for licensing.

The interesting observations show that

AM inhibits insulin secretion in a dosedependent manner. Further experiments

have shown that a neutralizing antibody

up-regulates insulin release at least fivefold, an effect that is reversed with the

addition of synthetic AM.

Novel Inhibitors of p53 for Treatment of

Neurodegenerative Disorders,

Myocardial Infarction and Other Tissue

Insults

Nigel H. Greig, et al. (NIA)

Serial No. 60/216,388, filed July 6, 2000

Licensing Contact: Norbert Pontzer;

301/496–7736, ext. 284; e-mail:

pontzern@nih.gov

The tumor suppressor protein p53 is

a key modulator of stress responses, and

activation of p53 precedes apoptosis

(programmed cell death) in many cell

types. Conditions that stress tissue, such

as deposition of amyloid b-peptide, may

thus cause tissue degeneration through

activation or up-regulation of p53. This

invention provides novel inhibitors of

p53 and methods of using these

inhibitors for the prevention or

treatment of the stress related tissue

degeneration observed in Alzheimer’s

disease, myocardial infarction and

stroke. In vitro and ex vivo studies

demonstrated that p53 inhibition

protected nerve cells from toxic insults

that otherwise induced programmed cell

death. In a rat model of stroke, p53

inhibition produced a 50% reduction in

stroke volume.

Dated: May 17, 2001.

Jack Spiegel,

Director, Division of Technology Development

and Transfer, Office of Technology Transfer,

National Institutes of Health.

[FR Doc. 01–13346 Filed 5–25–01; 8:45 am]

BILLING CODE 4140–01–P

DEPARTMENT OF HEALTH AND

HUMAN SERVICES

National Institutes of Health

National Heart, Lung, and Blood

Institute; Notice of Closed Meeting

Pursuant to section 10(d) of the

Federal Advisory Committee Act, as

amended (5 U.S.C. Appendix 2), notice

is hereby given of the following

meeting.

The meeting 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: National Heart, Lung,

and Blood Institute Special Emphasis Panel

NHLBI, National Research Service Training,

SEP (K’s).

Date: June 28–29, 2001.

Time: 7 PM to 5 PM.

Agenda: To review and evaluate grant

applications.

Place: Chevy Chase Holiday Inn, 5520

Wisconsin Ave., Chevy Chase, MD 20815.

Contact Person: Roy L. White, Phd, Review

Branch, NIH, NHLBI, Rockledge Building II,

6701 Rockledge Drive, Room 7196, Bethesda,

MD 20892, 301–435–0291.

(Catalogue of Federal Domestic Assistance

Program Nos. 93.233, National Center for

Sleep Disorders Research; 93.837, Heart and

Vascular Diseases Research; 93.838, Lung

Diseases Research; 93.839, Blood Diseases

and Resources Research, National Institutes

of Health, HHS)

Dated: May 22, 2001.

LaVerne Y. Stringfield,

Director, Office of Federal Advisory

Committee Policy.

[FR Doc. 01–13335 Filed 5–25–01; 8:45 am]

BILLING CODE 4140–01–M

DEPARTMENT OF HEALTH AND

HUMAN SERVICES

National Institutes of Health

National Heart, Lung, and Blood

Institute; Notice of Closed Meeting

Pursuant to section 10(d) of the

Federal Advisory Committee Act, as

amended (5 U.S.C. Appendix 2), notice

is hereby given of the following

meeting.

The meeting 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: National Heart, Lung,

and Blood Institute Special Emphasis Panel

ACTION–A–CHF trial Investigating

Outcomes, of Exercise Training.

Date: June 19, 2001.

Time: 2 to 5.

Agenda: To review and evaluate grant

applications.

Place: 5520 Wisconsin Avenue, Chevy

Chase, MD 20815.

Contact Person: Joyce A. Hunter, PhD,

Review Branch, Room 7194, Division of

Extramural Affairs, National Heart, Lung, and

Blood Institute, National Institutes of Health,

Bethesda, MD 20872.

This notice is being published less than 15

days prior to the meeting due to the timing

limitations imposed by the review and

funding cycle.

(Catalogue of Federal Domestic Assistance

Program Nos. 93.233, National Center for

Sleep Disorders Research; 93.837, Heart and

Vascular Diseases Research; 93.838, Lung

Diseases Research; 93.839, Blood Diseases

and Resources Research, National Institutes

of Health, HHS)

Dated: May 22, 2001.

LaVerne Y. Stringfield,

Director, Office of Federal Advisory

Committee Policy.

[FR Doc. 01–13336 Filed 5–25–01; 8:45 am]

BILLING CODE 4140–01–M

DEPARTMENT OF HEALTH AND

HUMAN SERVICES

National Institutes of Health

National Heart, Lung, and Blood

Institute; Notice of Closed Meeting

Pursuant to section 10(d) of the

Federal Advisory Committee Act, as

amended (5 U.S.C. Appendix 2), notice

is hereby given of the following

meeting.

The meeting 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.