Granted Patent B2

US 12,303,556 · App. 17/415,796 · Granted May 20, 2025

Inventor: Vincent Marion (Lipsheim, FR)

Assignees: UNIVERSITE DE STRASBOURG; INSERM (INSTITUT NATIONAL DE LA SANTÉ ET DE LA RECHERCHE MÉDICALE)

A61K38/45A61K45/06A61P3/10

Abstract

Claims (39)

1. A method of treating diabetes and associated disorders selected from the group consisting of type I diabetes, type II diabetes, insulin resistance, diabetic retinopathy, diabetic neuropathy, diabetic nephropathy, hyperglycemia, hyperinsulinaemia and Bardet Biedl syndrome comprising the administration of a peptide to a subject in need of treatment, wherein:

the peptide does not simultaneously comprise methionine, proline and arginine residues;

the peptide adopts a secondary structure which is a helix or an alpha helix;

the peptide has a length from 12 to 60 amino acids; and

wherein the peptide sequence comprises one of the following sequences:

(SEQ ID NO: 27)

VECTX X EKXVLA X ;

(SEQ ID NO: 28)

VECTX X EKXVLA X LDKXXFLTQLHS;

wherein the residues which are bold and underlined X carry a stapling and is any amino acid derivative suitable for stapling; and

wherein X is any amino acid except M, P and R.

2. The method according to claim 1 , wherein the peptide has a length of at least 12 amino acids and less than 40 amino acids.

3. The method according to claim 1 , wherein the peptide sequence comprises one of the following sequences:

(SEQ ID NO: 53)

VECTT X EKEVLA X LDKAAFLTQHS; or

(SEQ ID NO: 54)

VECTT X EKEVLA X LDKAAF;

wherein the residues which are bold and underlined X carry the stapling and is any amino acid derivative suitable for stapling; and

wherein X is any amino acid except M, P and R.

4. The method according to claim 3 , wherein X is an amino acid favorable to an α-helix secondary structure, or an amino acid selected from the group consisting of A, D, N, C, G, Q, E, H, L, K, F, S, W and Y.

5. The method according to claim 3 , wherein the first bold and underlined X is 2-(7-octenyl) arginine and the second bold and underlined X is 2-(4-pentenyl) serine, respectively, and said first and second X carry the stapling.

6. The method according to claim 1 , wherein the peptide sequence comprises:

(SEQ ID NO: 53)

VECTT X EKEVLA X LDKAAFLTQLHS,

wherein the first bold and underlined X is 2-(7-octenyl) arginine and the second bold and underlined X is 2-(4-pentenyl) serine, and said first and second X carry the stapling.

7. The method according to claim 1 , wherein the peptide is used in combination with one or more additional active drugs selected from the group consisting of an anti-diabetic drug, a hypolipidemic agent, an anti-obesity agent, an anti-hypertensive agent, an anti-steatotic drug, an anti-inflammatory agent, and an agonist of peroxisome proliferator-activator receptors.

8. The method according to claim 2 , wherein the peptide has a length of at least 12 amino acids and less than 25 amino acids.

9. The method according to claim 2 , wherein the peptide has a length of at least 12 amino acids and less than 30 amino acids.

10. The method according to claim 3 , wherein the peptide sequence consists of one of the following sequences:

(SEQ ID NO: 27)

VECTX X EKXVLA X ;

(SEQ ID NO: 28)

VECTX X EKXVLA X LDKXXFLTQLHS;

(SEQ ID NO: 53)

VECTT X EKEVLA X LDKAAFLTQHS; or

(SEQ ID NO: 54)

VECTT X EKEVLA X LDKAAF;

wherein the residues which are bold and underlined X carry the stapling and is any amino acid derivative suitable for stapling; and

wherein X is any amino acid except M, P and R.

Assignments (1)

Priority Claims (1)

Continuity (1)

References Cited (19)