Indiana University

Purdue Research Foundation

Merck Sharp + Dohme Corp.

Msd Italia S.r.l.

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

Brian P Ward

Richard Dennis DiMarchi

Alyssa Panitch

Brandon Seal

David L Smiley

Elisabetta Bianchi

Antonello Pessi

James Harold Patterson

Jonathan Wesley Day

Alessia Santoprete

Joseph M Metzger

Paul E Carrington

Joseph Chabenne

Maria DiMarchi

Paolo Ingallinella

Donald J Marsh

George J Eiermann

Ranabir Sinha Roy

Elena Capito

Alessandro Pocai

Richard Dimarchi

Ma Tao

The present invention provides polypeptide inhibitors of HSP27 kinase, compositions thereof, and methods for using such polypeptides and compositions for various therapeutic uses.

Polypeptide inhibitors of HSP27 kinase and uses therfor

Peptide analogs of oxyntomodulin (OXM, glucagon-37), which have been modified to be resistant to cleavage and inactivation by dipeptidyl peptidase IV (DPP-IV) and to increase in vivo half-life of the peptide analog while enabling the peptide analog to act as a dual GLP-1/glucagon receptor (GCGR) agonist are described. The peptide analogs are useful for treatment of metabolic disorders such as diabetes and obesity.

Oxyntomodulin analogs

Provided herein are glucagon analogs which exhibit potent activity at the GIP receptor, and, as such are contemplated for use in treating diabetes and obesity. In exemplary embodiments, the glucagon analog of the present disclosures exhibit an EC50 at the GIP receptor which is within the nanomolar or picomolar range.

Glucagon analogs exhibiting GIP receptor activity

The present invention relates to kinase inhibiting compositions and uses thereof. The invention further provides isolated kinase inhibiting peptides and uses thereof for inhibiting hyperplasia, for inhibiting the growth of neoplasms, and for inducing programmed cell death in a cell population.

Kinase inhibitors and uses thereof

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).

Glucagon/GLP-1 receptor co-agonists

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Lebanon, IN, United States of America

Brian P Ward