Eli Lilly and Company

Indiana University

Istituto Di Recerche Di Biologia Molecolare P. Angeletti S.r.l.

Msd Italia S.r.l.

Jonathan Wesley Day

Richard Dennis DiMarchi

David L Smiley

Maria DiMarchi

Joseph Chabenne

Gregory Alan Lazar

James Harold Patterson

Craig Duane Dickinson

Andrew Ihor Korytko

Robert William Siegel

John Michael Beals

Qing Chai

Robert John Konrad

Oliver Schroeder

David Bruce Baldwin

Yuewei Qian

James David Pancook

Avinash Muppidi

Josef George Heuer

Wei Ni

Elisabetta Bianchi

Antonello Pessi

Brian P Ward

Richard D Dimarchi

Maria Dimarchi

Brian C Ward

Ma Tao

Angiopoietin-like protein (ANGPTL)3/8 complexes and antibodies are disclosed, where the antibodies bind to and thereby neutralize ANGPTL3/8 complexes. Pharmaceutical compositions also are disclosed that include one or more anti-ANGPTL3/8 complex antibodies herein in a pharmaceutically acceptable carrier. Methods of making and using the same also are disclosed, especially for increase lipoprotein lipase activity and lowering triglycerides. In this manner, the compounds and compositions may be used in treating lipid metabolism-related and glucose metabolism-related diseases and disorders.

Anti-ANGPTL 3/8 complex antibodies and methods of using the same

The present invention relates to neuregulin (NRG) 4 compounds and methods of treatment with NRG4 compounds.

Neuregulin-4 compounds and methods of use

The present invention relates to fusion proteins comprising an insulin receptor agonist fused to a human IgG Fc region through the use of a peptide linker, and the use of such fusion proteins in the treatment of diabetes. The fusion protein of the present invention has an extended time action profile and is useful for providing basal glucose control for an extended period of time.

Fusion proteins

Angiopoietin-like protein (ANGPTL)3/8 fusion proteins are disclosed. Nucleic acid constructs encoding ANGPTL3/8 fusion proteins also are disclosed. Methods of making and using the same also are disclosed, especially for generating antibodies against ANGPTL3 and/or ANGPTL8.

Polynucleotides for preparing ANGPTL 3/8 complexes

Fusion proteins and methods of use

Anti-ANGPTL &#x215c; complex antibodies and methods of using the same

Angiopoietin-like protein (ANGPTL)3/8 complexes and antibodies are disclosed, where the antibodes bind to and thereby neutralize ANGPTL3/8 complexes. Pharmaceutical compositions also are disclosed that include one or more anti-ANGPTL3/8 complex antibodies herein in a pharmaceutically acceptable carrier. Methods of making and using the same also are disclosed, especially for increase lipoprotein lipase activity and lowering triglycerides. In this manner, the compounds and compositions may be used in treating lipid metabolism-related and glucose metabolism-related diseases and disorders.

ANGPTL3/8 complexes and methods of using the same

Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Glucagon/GLP-1 receptor co-agonists

Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).

Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (K-RNRNNIA) and SEQ ID NO: 28 (KRNR).

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Carmel, IN, United States of America

Jonathan Wesley Day