Fc–Fatty Acid Conjugate Platform for Extended Polypeptide Half-Life

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Solution Overview

Problem

Classical polypeptide drugs have short plasma half-lives due to rapid degradation by proteases and poor stability, limiting their clinical application and requiring frequent administration.

Innovation Solution

Conjugating biologically active molecules with an Fc-region of immunoglobulin and a modified fatty acid chain (C14-24) to form an ultra-long-acting platform, allowing direct or indirect binding to FcRn, increasing serum half-life and reducing renal excretion.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If polypeptide drugs are administered to maintain clinically effective concentrations, then therapeutic efficacy is improved, but administration frequency increases and patient burden increases

Engineering Contradiction:
Improvetherapeutic efficacyVSAvoidadministration frequency
Core Design Contradiction:
ReliabilityVSLoss of time

Solution Approach 1:

The patent merges the polypeptide drug with an Fc region of immunoglobulin to create a fusion protein. This combination leverages the Fc region's ability to bind FcRn receptors for prolonged circulation, thereby extending the half-life of the polypeptide drug and reducing administration frequency while maintaining therapeutic efficacy

Inventive Principle:
Principle #5Merging (Combining)

Solution Approach 2:

The invention creates a composite molecular structure combining the polypeptide active molecule with the Fc region. This composite structure exploits the complementary properties of both components: the therapeutic activity of the polypeptide and the extended circulation properties of the Fc region, achieving both sustained efficacy and reduced dosing frequency

Inventive Principle:
Principle #40Composite materials

2Stability of the object's composition

If polypeptide drugs are modified with conventional methods, then stability is improved, but half-life extension is limited

Engineering Contradiction:
Improvedrug stabilityVSAvoidplasma half-life
Core Design Contradiction:
Stability of the object's compositionVSDuration of action of moving object

Solution Approach 1:

The patent combines polypeptide drug modification with Fc region fusion, merging stability enhancement through proper folding and structural integrity with half-life extension through FcRn-mediated recycling, achieving both improved stability and extended duration of action simultaneously

Inventive Principle:
Principle #5Merging (Combining)

Solution Approach 2:

The invention changes the molecular parameters of the polypeptide drug by fusing it with the Fc region, fundamentally altering the drug's interaction with the immune system and enabling extended circulation through FcRn binding, thereby achieving significant half-life extension beyond conventional modification methods

Inventive Principle:
Principle #35Parameter changes

3Duration of action of moving object

If Fc-fusion proteins are used to extend half-life, then circulation time is improved, but molecular size increases

Engineering Contradiction:
Improveserum half-lifeVSAvoidmolecular size
Core Design Contradiction:
Duration of action of moving objectVSWeight of moving object

Solution Approach 1:

The patent extracts only the essential Fc region from the complete immunoglobulin molecule, using this extracted portion to achieve the desired half-life extension without incorporating the entire antibody structure, thereby minimizing the increase in molecular size while maintaining the circulation time benefit

Inventive Principle:
Principle #2Taking out (Extraction)

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The conjugated molecules exhibit extended circulation time, improved stability, and reduced immunogenicity, enhancing therapeutic potential by increasing target tissue exposure and reducing administration frequency.

Implementation Method 1

When entering into the acidified endosome after being uptaken by endothelial cells, the Fc-fusion protein is protected from lysosomal degradation via the binding of Fc to FcRn in the endosome

Methodology Applied
Scientific EffectFcRn binding:

Implementation Method 2

the serum half-life of the polypeptide drug is increased by the reversible binding of the fatty acid to serum albumin

Methodology Applied
Scientific EffectAlbumin binding:

Implementation Method 3

for a product with a molecular weight of less than 60 kDa, it would be readily cleared by the kidney, causing a short serum half-life; conjugating or fusing to the Fc-region will increase the size of the product, thus exceed the renal filtration threshold

Methodology Applied
Scientific EffectRenal filtration:

Data Source

PatentEP4595977A1Ultra-long-acting platform comprising fc-advanced fatty acid chain
Publication Date: 2025.08.06 WATERSTONE PHARMA (WUHAN) CO LTD
  • EP4595977A1 patent drawingFigure 1~2
  • EP4595977A1 patent drawingFigure 3~4B
  • EP4595977A1 patent drawingFigure 4C~5

AI summary

The present invention relates to an ultra-long-acting platform for improving the half-life of an active molecule of a drug, which comprises immunoglobulin Fc and an advanced advanced fatty acid chain. The present invention also relates to preparation of the conjugate platform, a composition compsring the conjugate, and a treatment application thereof. The present invention specifically relates to a conjugated molecule having a structure of "active molecule-Fc-Cn", wherein the active molecule is selected from any molecules beneficial to an organism, Fc is immunoglobulin IgG Fc, and Cn is a modified moiety comprising a C14-24 fatty acid chain. The present invention also relates to preparation of the conjugated molecule, a composition compsring the conjugate and a treatment application thereof.