Antiviral Peptide Combining VSV Transmembrane and Cell-Penetrating Sequences
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Solution Overview
Problem
Current treatments for viral diseases are limited due to the lack of effective vaccines and antiviral agents, and the emergence of drug-resistant viruses complicates therapeutic options, necessitating the development of antiviral agents with different functional mechanisms and chemical characteristics.
Innovation Solution
A novel artificial antiviral peptide is designed, combining a transmembrane sequence from the vesicular stomatitis virus (VSV) glycoprotein with a cell-penetrating peptide sequence, which exhibits excellent antiviral activity by inhibiting virus proliferation and infection.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If conventional antiviral treatments are used, then existing therapeutic options are available, but drug-resistant viruses emerge and treatment effectiveness decreases
Solution Approach 1:
The invention changes the chemical and functional parameters of antiviral agents by using synthetic peptides with novel structures (combining transmembrane sequences from VSV glycoproteins with cell-penetrating peptide sequences) that differ fundamentally from conventional antiviral drugs, thereby overcoming drug resistance through mechanistic novelty rather than incremental modification
Solution Approach 2:
The antiviral peptide is constructed as a composite structure combining two functional sequences: a transmembrane sequence (TM sequence) from VSV glycoprotein that provides membrane interaction capability, and a cell-penetrating peptide sequence (CPP sequence) that enables cellular uptake. This composite structure creates a novel antiviral mechanism that bypasses existing drug resistance
2Reliability
If naturally derived antiviral peptides are used, then antiviral activity is achieved, but structural novelty and patentability are limited
Solution Approach 1:
The antiviral peptide is segmented into two distinct functional domains: the transmembrane sequence portion (amino acid residues 1-19 or variants) derived from VSV glycoprotein that mediates membrane insertion and disruption, and the cell-penetrating peptide sequence (such as TAT, penetratin, or poly-arginine) that facilitates cellular internalization. This segmentation allows independent optimization of each function while creating a novel chimeric structure
Solution Approach 2:
The cell-penetrating peptide sequence acts as an intermediary that mediates the delivery of the transmembrane sequence into host cells. The CPP sequence enables the hydrophobic transmembrane portion to cross cellular membranes without causing premature aggregation or toxicity, thereby facilitating the antiviral mechanism while maintaining cell viability
3Reliability
If peptide length is increased to improve antiviral activity, then viral inhibition effectiveness increases, but production cost and synthesis difficulty increase
Solution Approach 1:
The transmembrane sequence is truncated to the essential minimal length (19 amino acids or fewer) required for membrane insertion and antiviral activity, rather than using the full-length glycoprotein sequence. This partial action approach retains sufficient antiviral function while dramatically reducing synthesis complexity and cost
Solution Approach 2:
The cell-penetrating peptide sequence provides universal cellular uptake capability that can be combined with various transmembrane sequences from different viral strains or even different viruses, allowing a single CPP module to serve multiple antiviral applications and reducing the need for extensive peptide optimization
Data Source
AI summary
An antiviral peptide provided according to the present invention includes (1) an amino acid sequence (TM sequence) constituting a transmembrane region of G protein of vesicular stomatitis virus (VSV) or a modified amino acid sequence formed by conservative substitutions of 1, 2, or 3 amino acid residues in the TM sequence; and (2) an amino acid sequence (CPP sequence) functioning as a cell penetrating peptide (CPP), wherein a total number of amino acid residues is 100 or less.