Cell-Penetrating Peptide Fragment for Efficient Cargo Transfer
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Solution Overview
Problem
Existing cell-penetrating peptides face challenges in efficiently transferring foreign substances such as nucleic acids, polypeptides, and drugs across eukaryotic cell membranes.
Innovation Solution
A peptide fragment with an amino acid sequence RRRRSNRRG (SEQ ID No.: 1) is developed, which exhibits enhanced cell membrane permeability, allowing constructs with this peptide to efficiently transfer foreign substances like polypeptides, nucleic acids, and drugs into eukaryotic cells.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If conventional cell-penetrating peptides are used to transfer foreign substances into cells, then cell membrane permeability is achieved, but transferring efficiency is insufficient
Solution Approach 1:
The patent modifies the amino acid sequence parameters of conventional cell-penetrating peptides by inserting a serine-asparagine (SN) dipeptide at specific positions. This parameter change in the peptide structure fundamentally alters its interaction with cell membranes, transforming it from a mere membrane penetrator to an efficient intracellular delivery vehicle that maintains permeability while dramatically improving transferring efficiency.
Solution Approach 2:
The invention creates a composite functional peptide by combining the membrane-penetrating capability of conventional CPPs with the enhanced delivery properties of the SN-containing sequence. This composite structure integrates multiple functions: membrane penetration, cargo binding, and efficient intracellular transfer, resolving the contradiction between permeability and transferring efficiency.
2Stability of the object's composition
If peptide length is increased to improve stability, then structural stability is enhanced, but cell membrane permeability may be reduced
Solution Approach 1:
The patent segments the peptide structure into functional domains: the core CPP sequence responsible for membrane penetration, and the strategically placed SN dipeptide segments that enhance stability and transferring efficiency. This segmentation allows each part to optimize its function without compromising the other, maintaining permeability while improving structural stability.
Solution Approach 2:
The invention applies local quality modification by specifically inserting the SN dipeptide at predetermined positions within the peptide sequence rather than uniformly increasing peptide length. This localized modification provides structural stability enhancement at critical positions while preserving the overall compact structure necessary for cell membrane permeability.
Data Source
Figure 1

AI summary
A peptide fragment disclosed herein includes an amino acid sequence: RRRRSNRRG (SEQ ID No.: 1), in which a total of amino acid residues is 10 or less.