Antimicrobial Peptides via Laminin Binding Site and Basic Sequence
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Conventional antimicrobial peptides isolated from nature have limitations in exceeding natural antimicrobial activity and spectrum, making it difficult to develop agents with enhanced performance.
Innovation Solution
Artificially designed antimicrobial peptides with unique amino acid sequences, specifically combining laminin binding site sequences and high basic partial sequences, are synthesized to exhibit broad antimicrobial activity against bacteria and fungi.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional antimicrobial peptides isolated from nature are used, then broad antimicrobial spectrum is achieved, but antimicrobial performance cannot exceed natural activity levels
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence parameters of natural peptides. Specifically, it combines the laminin binding site sequence (LMWWML or variants) with high-basic sequence motifs (such as RKKKRKV) to create novel peptide sequences that maintain cell recognition functionality while enhancing antimicrobial activity through optimized charge distribution and structural properties.
Solution Approach 2:
The patent employs composite materials principle by creating hybrid peptides that combine two distinct functional sequences: the laminin binding site sequence (providing cell recognition and binding capability) and the high-basic sequence (providing enhanced antimicrobial activity). This composite structure integrates the advantages of both sequence types to achieve superior antimicrobial performance while maintaining biological specificity.
2Reliability
If artificially designed amino acid sequences are created, then enhanced antimicrobial activity is achieved, but deviation from natural sequences increases production complexity
Solution Approach 1:
The patent applies segmentation by dividing the antimicrobial peptide into two distinct functional segments: the laminin binding site sequence (LMWWML or保守性替换变体) and the high-basic sequence motif. This segmentation allows each segment to be independently optimized for its specific function while simplifying the overall design and production process, as each segment can be separately synthesized and then combined.
Solution Approach 2:
The patent utilizes universality by designing a modular peptide structure where the laminin binding site sequence provides universal cell recognition functionality across different applications, while the high-basic sequence provides universal antimicrobial activity. This multi-functional design allows the same basic structure to be applied across various antimicrobial applications with minimal modification.
Data Source
AI summary
Antimicrobial peptide provided by present invention is an artificially designed antimicrobial peptide that does not occur naturally, and includes a sequence composed of at least 6 contiguous amino acid residues selected from an amino acid sequence constituting laminin binding site (LBS), or said sequence with one or a plurality of amino acid residue(s) conservatively replaced, and an amino acid sequence that can express antimicrobial activity against at least one kind of bacteria or fungi. It is desirable that the total number of amino acid residues is 100 or less.