A fusion peptide comprising a GLP1 variant, and at least one adiponectin agonist peptide which is chemically attached to the GLP1 variant via by a spacer. The GLP1 variant portion can include one or more substitutions relative to the native GLP1. The adiponectin agonist peptide can be attached to the GLP1 variant at different attachment sites. A method of treating a metabolic disorder or condition using the fusion peptide is also provided.

A fusion peptide comprising a GLP1 variant, and at least one adiponectin agonist peptide which is chemically attached to the GLP1 variant via by a spacer. The GLP1 variant portion can include one or more substitutions relative to the native GLP1. The adiponectin agonist peptide can be attached to the GLP1 variant at different attachment sites. A method of treating a metabolic disorder or condition using the fusion peptide is also provided.

The invention relates to a method for the cleavage of a solid phase-bound polypeptide from the solid phase, the method comprising contacting the solid phase, to which the polypeptide is bound, with a composition consisting essentially of trifluoroacetic acid and 1,2-ethanedithiol, at a temperature in the range of about 23° C. to about 29° C.

The invention relates to a method for the cleavage of a solid phase-bound polypeptide from the solid phase, the method comprising contacting the solid phase, to which the polypeptide is bound, with a composition consisting essentially of trifluoroacetic acid and 1,2-ethanedithiol, at a temperature in the range of about 23° C. to about 29° C.

A method for producing a dual function protein includes a biologically active protein and an FGF21 mutant protein. The method allows stable production of a target protein by effectively preventing decomposition of the target protein, and thus has a high potential for commercial usage.

A method for producing a dual function protein includes a biologically active protein and an FGF21 mutant protein. The method allows stable production of a target protein by effectively preventing decomposition of the target protein, and thus has a high potential for commercial usage.

Prodrug compounds of GLP-1/GIP receptor co-agonists are provided wherein the GLP-1/GIP receptor co-agonists have been modified by the linkage of a dipeptide to the GLP-1/GIP receptor co-agonist through an amide bond. The prodrugs disclosed herein have extended half-lives and are converted to the active GLP-1/GIP receptor co-agonist at physiological conditions through a non-enzymatic reaction driven by chemical instability.

Prodrug compounds of GLP-1/GIP receptor co-agonists are provided wherein the GLP-1/GIP receptor co-agonists have been modified by the linkage of a dipeptide to the GLP-1/GIP receptor co-agonist through an amide bond. The prodrugs disclosed herein have extended half-lives and are converted to the active GLP-1/GIP receptor co-agonist at physiological conditions through a non-enzymatic reaction driven by chemical instability.

The present invention relates to a facile acylation process for preparation of N-Substituted peptide and proteins. More specifically, the invention relates to acylating a peptide or a protein with deprotected acylating agent.

Provided herein are methods of improving glycemic control, reducing weight, and/or treating type 2 diabetes mellitus in human patients comprising administering GLP-1/glucagon agonist peptides, dapagliflozin, and metformin.