RBD-Binding Peptide Sequence for Stronger COVID-19 Viral Entry Blocking
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Solution Overview
Problem
Existing peptide therapeutic agents for COVID-19 are not effective in strongly binding to the receptor binding domain (RBD) of the SARS-CoV2 virus, limiting their ability to prevent viral entry into human cells.
Innovation Solution
A novel peptide with an amino acid sequence (SEQ ID NO: 1) designed to bind specifically to the RBD, incorporating additional interactions with charged amino acids D420 and K458, enhancing binding affinity and stability.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing peptide therapeutic agents are used to bind to RBD, then they can provide some level of viral neutralization, but their binding affinity is insufficient to strongly prevent viral entry
Solution Approach 1:
The peptide sequence was optimized by changing specific amino acid parameters to enhance binding affinity. The patent identifies specific amino acid positions and substitutions that improve the peptide's ability to bind to RBD, directly addressing the insufficient binding affinity of existing peptides
Solution Approach 2:
The invention creates a composite peptide structure that combines multiple functional elements: an N-terminal region for RBD binding, a proline-rich region for structural stability, and a C-terminal region for additional interactions. This composite design achieves stronger overall binding affinity than previous single-function peptides
2Reliability
If peptide sequence is optimized for stronger RBD binding, then binding affinity improves, but the complexity of design and validation increases
Solution Approach 1:
The peptide is divided into distinct functional segments: an N-terminal binding region (amino acids 1-15) that specifically interacts with RBD, a middle proline-rich region (amino acids 16-30) that provides structural stability, and a C-terminal region that enhances binding. This segmentation allows independent optimization of each region's function
Solution Approach 2:
Specific amino acid positions within the peptide are optimized with particular properties for specific functions. For example, proline residues are placed at specific positions to induce beta-turn structures that enhance RBD binding, while charged amino acids are positioned to form salt bridges with complementary residues on RBD
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 novel peptide exhibits stronger binding to the RBD, potentially inhibiting viral entry and serving as a more effective therapeutic agent for COVID-19.
Implementation Method 1
the peptide of the present disclosure includes a new portion added with a novel amino acid sequence fundamentally designed for interaction in the dimension of atoms consisting of the amino acids
Implementation Method 2
uniquely designing an expanded peptide capable of additionally interacting with charged amino acids of D420 and K458
Data Source
AI summary
The present invention relates to a peptide for treatment of the corona virus infection COVID-19 and a use thereof. In order to make the binding to the new epitope of SARS-CoV2 RBD stronger compared to the peptide (P6) simulating the conventionally known binding site between SARS-CoV RBD and ACE2, the peptide of the present invention includes a new portion added with a novel amino acid sequence fundamentally designed for interaction in the dimension of atoms consisting of the amino acids. Suggested in the present invention is a novel design of a peptide having higher binding affinity than conventionally known peptides, wherein an expanded peptide is creatively designed to additionally interact with charged amino acids of D420 and K458, located at the rear side of the known binding boundary between RBD and hACE2. The peptide of the present invention exhibits high possibility as a therapeutic agent for COVID-19.