BMP-Binding Peptide for Reproducible Stem Cell Differentiation Control
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Existing growth factor inhibitors like Noggin, Chordin, and follistatin are costly and have poor reproducibility for regulating stem cell culture, particularly in inhibiting BMP signal transduction and controlling stem cell differentiation.
Innovation Solution
Development of novel peptides with specific amino acid sequences, such as SEQ ID NO: 1 and SEQ ID NO: 2, that exhibit BMP binding activity and inhibit BMP signal transduction, allowing for regulation of stem cell differentiation.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If Noggin, Chordin, or follistatin are used as BMP inhibitors in stem cell culture, then BMP signal transduction is inhibited and stem cell differentiation is regulated, but culture costs increase and reproducibility deteriorates
Solution Approach 1:
The patent creates simplified peptide copies of the functional domains of Noggin, Chordin, and follistatin. These peptides replicate the BMP-binding capability of the full-length proteins but with reduced complexity, resulting in lower production costs and improved batch-to-batch reproducibility while maintaining the essential inhibitory function
Solution Approach 2:
The invention extracts only the critical BMP-binding regions from the full-length Noggin, Chordin, and follistatin proteins. By isolating and synthesizing just these essential functional segments as peptides, the solution eliminates unnecessary protein complexity, reducing manufacturing costs and improving reproducibility while preserving the core BMP inhibition function
2Reliability
If Noggin, Chordin, or follistatin are used as BMP inhibitors, then stem cell differentiation is regulated, but manufacturing complexity and cost increase
Solution Approach 1:
The patent segments the full-length Noggin, Chordin, and follistatin proteins into smaller functional peptide units. By dividing these complex proteins into essential functional segments that retain BMP-binding activity, the invention reduces structural complexity while maintaining regulatory effectiveness in stem cell differentiation
Solution Approach 2:
The invention extracts only the essential BMP-binding functional domains from the complex protein structures of Noggin, Chordin, and follistatin. This extraction of core functional elements eliminates unnecessary structural complexity while preserving the ability to effectively regulate stem cell differentiation through BMP signal inhibition
3Reliability
If peptide sequences are modified through substitution, addition, deletion, or insertion of amino acid residues, then binding activity to BMP is maintained or improved, but sequence complexity increases
Solution Approach 1:
The patent applies local quality modifications by making targeted amino acid substitutions, additions, deletions, or insertions at specific positions within the peptide sequence. These localized modifications optimize BMP-binding activity at critical regions while maintaining overall sequence simplicity, rather than uniformly complicating the entire peptide structure
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 peptides effectively inhibit BMP4 and BMP7 signal transduction, providing a cost-effective and reproducible means to regulate stem cell differentiation, suitable for use in culture media supplements.
Implementation Method 1
the peptide having BMP4 binding ability and inhibitory activity of BMP4... The peptide or the pharmaceutically acceptable salt thereof has BMP7 signal transduction inhibitory activity
Data Source
AI summary
[Problem] To provide a novel peptide having a BMP4 binding ability. [Solution] The present invention pertains to a peptide and a peptide-containing agent. The peptide according to the present invention has an amino acid sequence of E-R-V-F4COO-Atp-D-R-Bph-P-Y-P-Bph-Y-F4COO-F4COO-S-C (SEQ ID NO: 1) or has an amino acid sequence resulting from substitution, addition, deletion, or insertion at 1-15 amino acid residues selected from the group consisting of amino acid residues at positions 1, 2, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, and 16 in said amino acid sequence.