GIP Receptor Activating Peptide Sequence Design

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Solution Overview

Problem

Current peptide compounds do not effectively target GIP receptors for therapeutic or preventive agents for diabetes, obesity, and related conditions such as vomiting or nausea.

Innovation Solution

Development of novel peptide compounds with specific sequences that selectively activate GIP receptors, demonstrating significant hypoglycemic and antiemetic actions.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Adaptability or versatility

If peptide compounds are designed based on natural glucagon, GIP, or GLP-1 structures, then GLP-1 receptor/GIP receptor coagonist or glucagon receptor/GLP-1 receptor/GIP receptor triagonist activity is achieved, but selective activation of GIP receptors is not obtained

Engineering Contradiction:
Improvereceptor coagonist/triagonist activityVSAvoidselective activation of GIP receptors
Core Design Contradiction:
Adaptability or versatilityVSMeasurement precision

Solution Approach 1:

The patent segments the peptide structure into specific modular regions with defined amino acid sequences. By dividing the peptide into N-terminal, central, and C-terminal regions with specific residue requirements (e.g., positions 2-4, 10-12, 20-22), the invention achieves selective GIP receptor activation while maintaining structural organization for targeted receptor interaction.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The patent applies local quality by specifying particular amino acid properties at different positions within the peptide sequence. Certain positions require hydrophobic residues (e.g., phenylalanine, leucine), others require charged residues (e.g., lysine, arginine), and specific positions mandate proline or glycine to create local structural features that selectively engage GIP receptors with high precision.

Inventive Principle:
Principle #3Local quality

2Adaptability or versatility

If extensive modifications are made to achieve coagonist or triagonist activity, then broad receptor activity is obtained, but the peptide structure becomes complex and difficult to optimize for selective GIP receptor activation

Engineering Contradiction:
Improvebroad receptor activityVSAvoidpeptide structure complexity
Core Design Contradiction:
Adaptability or versatilityVSDevice complexity

Solution Approach 1:

The patent systematically changes peptide parameters including amino acid composition, sequence length (25-40 residues), disulfide bridge positioning, and N/C-terminal modifications to optimize GIP receptor selectivity. By controlling parameters such as hydrophobicity at specific positions and charge distribution, the invention achieves selective activation without requiring excessive structural complexity.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates composite peptide structures combining hydrophobic regions, charged regions, and rigid proline-glycine motifs in a single sequence. This composite approach integrates multiple functional elements that work synergistically to achieve selective GIP receptor binding while maintaining a manageable structural framework rather than requiring separate molecular components.

Inventive Principle:
Principle #40Composite materials

Data Source

PatentEP3601329B1GIP receptor activating peptide
Publication Date: 2024.12.04 TAKEDA PHARMA CO LTD
  • EP3601329B1 patent drawingFigure 1-1~1-2
  • EP3601329B1 patent drawingFigure 2-1~2-2
  • EP3601329B1 patent drawingFigure 2-3

AI summary

The present invention provides a novel peptide compound having an activating action on GIP receptors and use of the peptide compound as a medicament. Specifically, a peptide containing a sequence represented by the formula (I) or a salt thereof and a medicament comprising the same are provided. P1-Tyr-A2-Glu-Gly-Thr-A6-A7-A8-A9-A10-A11-A12-A13-A14-A15-A16-A17-A18-A19-A20-A21-A22-A23-A24-A25-A26-A27-A28-A29-A30-A31-A32-A33-A34-A35-A36-A37-A38-A39-A40-P2 (I) wherein each symbol is as defined herein.