Peptide-Selective Antimicrobial Textile to Preserve Skin Microbiome

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Solution Overview

Problem

Current antimicrobial textiles that use broad-spectrum antimicrobials can harm beneficial skin bacteria, leading to skin irritation and health issues, and these antimicrobials lose effectiveness quickly due to leaching and instability when encapsulated or bonded to surfaces.

Innovation Solution

Development of antimicrobial fabrics with peptides that selectively bind and kill specific odor-causing and pathogenic bacteria, such as Staphylococcus aureus, Pseudomonas aeruginosa, and Corynebacterium, while avoiding beneficial bacteria, using a composition that includes polyhexamethylene biguanidine (PHMB) and peptides covalently bound to the fabric surface using an EDC coupling reaction.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Object-affected harmful factors

If broad-spectrum antimicrobials are used in textiles, then odor control is improved, but skin microbiome health deteriorates

Engineering Contradiction:
Improveodor controlVSAvoidskin microbiome health
Core Design Contradiction:
Object-affected harmful factorsVSObject-generated harmful factors

Solution Approach 1:

The patent applies local quality by designing peptides with specific recognition sequences that target only particular pathogenic bacteria (such as S. aureus and P. aeruginosa) rather than acting broadly against all bacteria. This selective targeting allows the antimicrobial textile to control odor caused by specific pathogens while preserving beneficial skin microbiota, thus resolving the contradiction between effective odor control and skin health maintenance.

Inventive Principle:
Principle #3Local quality

2Adaptability or versatility

If encapsulated bacteriocins are used, then targeted antimicrobial activity is achieved, but activity is lost quickly due to leaching and instability

Engineering Contradiction:
Improvetargeted antimicrobial activityVSAvoidantimicrobial activity duration
Core Design Contradiction:
Adaptability or versatilityVSDuration of action of stationary object

Solution Approach 1:

The patent employs preliminary action by covalently bonding the peptide to the textile surface before use, creating a stable, long-lasting antimicrobial textile. The peptide is chemically attached to the fabric matrix in advance, ensuring it remains fixed and active throughout the textile's service life, thereby preventing leaching and maintaining targeted antimicrobial activity over extended periods.

Inventive Principle:
Principle #10Preliminary action

Solution Approach 2:

The patent utilizes composite materials by integrating the peptide with the textile substrate through covalent bonding, creating a hybrid structure where the peptide's antimicrobial function is permanently embedded in the fabric. This composite approach ensures the peptide remains stable and active, resolving the issue of rapid activity loss associated with encapsulated bacteriocins.

Inventive Principle:
Principle #40Composite materials

3Stability of the object's composition

If covalent bonding is used to attach antimicrobials, then stability is improved, but leaching still occurs and activity is lost

Engineering Contradiction:
Improveantimicrobial stabilityVSAvoidantimicrobial leaching
Core Design Contradiction:
Stability of the object's compositionVSLoss of substance

Solution Approach 1:

The patent applies the taking out principle by removing the problematic encapsulation layer and directly covalently bonding the peptide to the textile surface. This eliminates the interface between the antimicrobial and the external environment that would otherwise allow leaching, thereby maintaining stability while preventing substance loss.

Inventive Principle:
Principle #2Taking out (Extraction)

Solution Approach 2:

The patent uses an intermediary approach by employing a covalent bond as a permanent connector between the peptide and the textile substrate. This strong chemical linkage acts as an effective mediator that prevents the peptide from detaching or leaching, while maintaining the peptide's biological activity and stability throughout the textile's lifespan.

Inventive Principle:
Principle #24Intermediary (Mediator)

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 solution effectively targets and kills specific pathogens without affecting beneficial bacteria, maintaining antimicrobial activity for longer periods and reducing the need for frequent washing of protective uniforms.

Implementation Method 1

The peptide can be used to selectively bind and/or kill specific bacteria such as, but not limited to, Staphylococcus aureus, Pseudomonas aeruginosa, and Corynebacterium

Methodology Applied
Scientific EffectSelective binding:

Implementation Method 2

using a composition that includes polyhexamethylene biguanidine (PHMB) and peptides covalently bound to the fabric surface using an EDC coupling reaction

Methodology Applied
Scientific EffectCovalent bonding: Chemical Bonding

Implementation Method 3

an antimicrobial composition that kills the selectively bound odor causing and/or pathogenic bacteria

Methodology Applied
Scientific EffectAntimicrobial action:

Data Source

PatentUS11457625B1Tuning a broad acting antimicrobial textile to act as a narrow spectrum antimicrobial textile
Publication Date: 2022.10.04 UNITED STATES OF AMERICA THE AS REPRESENTED BY THE SEC OF THE ARMY
  • US11457625B1 patent drawing
  • US11457625B1 patent drawing
  • US11457625B1 patent drawing

AI summary

The disclosed subject matter relates to a textile or fabric and methods of making them that includes a composition that selectively binds odor causing and/or pathogenic bacteria, but avoids binding beneficial bacteria and an antimicrobial composition that kills the selectively bound odor causing and/or pathogenic bacteria. The composition that selectively binds odor causing and/or pathogenic bacteria can be a peptide.