Modified Polypeptides Amidation Acetylation Antibacterial Activity

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Solution Overview

Problem

Current polypeptide-based antibacterial agents have limited antibacterial activity compared to traditional antibiotics, necessitating the development of novel polypeptides with enhanced antibacterial and antifungal properties.

Innovation Solution

Modification of existing polypeptides by amidation and acetylation of the carboxyl-terminal and amino-terminal ends, respectively, to create polypeptides with improved antibacterial and antifungal activities, which can be used in various formulations for treating infections and as antiseptics.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If existing polypeptide structures are used, then the polypeptides can be produced, but their antibacterial activities are insufficient compared to traditional antibiotics

Engineering Contradiction:
Improveantibacterial activityVSAvoideffectiveness relative to antibiotics
Core Design Contradiction:
ReliabilityVSProductivity

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence of existing polypeptides (changing chemical composition parameters) and using site-directed mutagenesis to alter specific residues. This optimizes the polypeptide structure to enhance antibacterial activity, directly resolving the contradiction between producibility and effectiveness.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates composite polypeptide structures by combining different amino acid sequences and domains (e.g., fusion proteins containing VEGF-like activity and antibacterial domains). This composite approach enables the polypeptides to achieve superior antibacterial activity compared to natural polypeptides while maintaining producibility.

Inventive Principle:
Principle #40Composite materials

2Reliability

If polypeptides are modified to enhance antibacterial activity, then antibacterial effectiveness improves, but the complexity of the polypeptide structure increases

Engineering Contradiction:
Improveantibacterial activityVSAvoidpolypeptide structure complexity
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent segments polypeptide structures into functional domains (e.g., separate antibacterial domains and VEGF-like activity domains in fusion proteins). This segmentation allows each domain to perform its specific function while making the overall complex structure more manageable and producible through modular expression systems.

Inventive Principle:
Principle #1Segmentation

Solution Approach 2:

The patent designs multi-functional polypeptides that combine antibacterial activity with other functions (e.g., VEGF-like angiogenic activity). This universality allows a single modified polypeptide to address multiple therapeutic needs simultaneously, justifying the increased structural complexity through enhanced overall efficacy.

Inventive Principle:
Principle #6Universality (Multi-functionality)

Data Source

PatentEP2404932B1Polypeptides and antibacterial or antiseptic use of same
Publication Date: 2014.07.23 ANGES MG INC
  • EP2404932B1 patent drawing
  • EP2404932B1 patent drawing
  • EP2404932B1 patent drawing

AI summary

A novel polypeptide, and an antibacterial agent, antifungal agent and/or antiseptic containing as an effective ingredient the polypeptide are disclosed. The polypeptide of this invention has an amino acid sequence shown in SEQ ID NOs:1 to 12 and 13 to 31. This antibacterial agent, antifungal agent and/or antiseptic is useful for the prevention, amelioration or treatment of diseases such as burn, decubitus, wound, skin ulcer, leg ulcer, diabetic ulcer, occlusive arterial disease and arteriosclerosis obliterans, cellulitis, acute lymphangitis, lymphadenitis, erysipelas, skin abscess, necrotizing subcutaneous infection, staphylococcal scalded skin syndrome (SSSS), folliculitis, facial furuncle, suppurative hidradenitis, carbuncle, infectious paronychia, erythrasma and severe infection (sepsis).