Promininin-1 Peptide VEGF Binding Modification
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Solution Overview
Problem
Current methods for regulating angiogenesis are inadequate in addressing pathological conditions resulting from excessive or insufficient blood vessel formation, such as cancer, diabetic retinopathy, and vascular diseases, as they fail to effectively modulate the balance between angiogenic and angiostatic factors.
Innovation Solution
Development of modified peptides derived from prominin-1 that enhance VEGF binding and endothelial cell interaction, promoting angiogenesis and regenerative activities, including wound healing, tissue repair, and neuroprotection, by modifying the native peptide #237 with hydrophobic amino acid substitutions and conservative substitutions.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If native prominin-1 peptide is used, then basic VEGF binding activity is present, but binding activity and pro-angiogenic effect are insufficient for effective therapeutic intervention
Solution Approach 1:
The patent applies parameter changes by systematically modifying the amino acid sequence of the native prominin-1 peptide through conservative substitutions (replacing amino acids with chemically similar alternatives) and hydrophobic substitutions (introducing more hydrophobic amino acids). These parameter changes in the peptide structure result in modified peptides with enhanced VEGF binding activity and improved pro-angiogenic effects, directly resolving the insufficiency of the native peptide's therapeutic activity.
2Adaptability or versatility
If current angiogenesis regulation methods are used, then some level of vascular control is achieved, but they fail to effectively modulate the balance between angiogenic and angiostatic factors in pathological conditions
Solution Approach 1:
The patent applies local quality by creating peptide variants with specific localized modifications at particular positions in the sequence. Different modified peptides have enhanced activity at specific locations, allowing selective modulation of VEGF binding and pro-angiogenic effects. This localized optimization enables effective intervention in pathological conditions by targeting specific molecular interactions rather than relying on non-specific systemic effects.
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 modified peptides demonstrate enhanced VEGF-related binding activity, promoting angiogenesis, cell proliferation, and neuroprotection, offering therapeutic potential for conditions like wound healing, vascular diseases, and neurodegenerative disorders.
Implementation Method 1
Modified peptides described herein exhibit enhanced VEGF-related binding activity over that of a native non-modified prominin-1 peptide. The native peptide #237, having the sequence DRVQRQTTTVVA binds VEGF. Modified peptides described herein exhibit enhanced VEGF-related binding activity... by modifying the native peptide #237 with hydrophobic amino acid substitutions
Data Source
AI summary
Described have herein are peptide analogs of a prominin-1 peptide, DRVQRQTTTVVA (SEQ. ID. NO:1) which have enhanced regenerative and/or angiogenesis activity, increase VEGF binding to endothelial cells, and/or increase wound healing activity relative to the peptide of SEQ ID NO: 1. Provided herein are fusion proteins and compositions comprising these peptide analogs and uses thereof.