De Novo Chlorophyll Special Pair Proteins for Dimer Geometry

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Solution Overview

Problem

Existing methods struggle to systematically assemble chlorophyll dimers with predefined geometries that precisely match special pair geometries, hindering the development of synthetic biology for efficient solar-to-fuel energy conversion.

Innovation Solution

Design and synthesis of de novo chlorophyll special pair proteins with specific amino acid sequences that can bind to chlorophyll dimers, forming homodimers and scaffolds, and potentially incorporating functional domains for various applications.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If natural photosystems are used to study chlorophyll special pairs, then the native structure and function are preserved, but the complexity of natural photosystems makes it difficult to study these Chls directly

Engineering Contradiction:
Improvenative structure and functionVSAvoidcomplexity of natural photosystems
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The patent extracts and isolates the chlorophyll special pair from the complex natural photosystem context, creating simplified de novo designed proteins that contain only the essential chlorophyll binding functionality. This allows study of special pair properties without the complicating factors of complete photosystem complexes.

Inventive Principle:
Principle #2Taking out (Extraction)

Solution Approach 2:

The patent segments the complex photosystem into minimal functional units by designing proteins that bind only the chlorophyll special pair, separating the chlorophyll binding function from other photosystem components for independent study and optimization.

Inventive Principle:
Principle #1Segmentation

2Device complexity

If small molecule mimics of special pairs are used, then the structure is simplified, but they are labor-intensive to synthesize and overlook the role of protein matrix effects

Engineering Contradiction:
Improvestructure simplificationVSAvoidsynthesis complexity
Core Design Contradiction:
Device complexityVSEase of manufacture

Solution Approach 1:

The patent employs de novo protein design where the protein structure self-assembles to create the precise chlorophyll binding geometry, eliminating the need for labor-intensive chemical synthesis of complex small molecule mimics while maintaining structural precision.

Inventive Principle:
Principle #25Self-service

Solution Approach 2:

The patent changes the approach from chemical synthesis of small molecules to biological synthesis of proteins, utilizing the protein's three-dimensional structure to precisely position chlorophyll molecules, thereby simplifying manufacturing while maintaining and enhancing structural precision.

Inventive Principle:
Principle #35Parameter changes

3Ease of manufacture

If small molecule mimics are used, then synthesis is avoided, but they lack the fine control over Chl-Chl distances and orientations needed to reproduce the precise geometries of native special pairs

Engineering Contradiction:
Improvesynthesis avoidanceVSAvoidChl-Chl distance and orientation control
Core Design Contradiction:
Ease of manufactureVSManufacturing precision

Solution Approach 1:

The patent replaces chemical synthesis methods with protein-based structural control, where the three-dimensional protein fold mechanically positions chlorophyll molecules with atomic-level precision, achieving superior control over Chl-Chl distances and orientations compared to small molecule approaches.

Inventive Principle:
Principle #28Mechanics substitution (Replace mechanical system)

Solution Approach 2:

The patent creates a composite system where the protein matrix and chlorophyll molecules work together, with the protein's structured environment providing precise geometric control over the chlorophyll arrangement, achieving native-like special pair geometries that small molecule mimics cannot replicate.

Inventive Principle:
Principle #40Composite materials

4Manufacturing precision

If de novo designed proteins are created to bind chlorophyll dimers, then precise control over Chl-Chl distances and orientations is achieved, but no structures of Chl dimers in designed proteins have been determined experimentally

Engineering Contradiction:
ImproveChl-Chl distance and orientation controlVSAvoidexperimental structure determination
Core Design Contradiction:
Manufacturing precisionVSMeasurement precision

Solution Approach 1:

The patent employs iterative design-refinement cycles where computational models are continuously improved based on experimental feedback from X-ray crystallography and spectroscopy, allowing the structure to be refined to match the designed geometry with increasing precision in each iteration.

Inventive Principle:
Principle #23Feedback

Solution Approach 2:

The patent performs extensive computational modeling and simulation before experimental structure determination, pre-optimizing the protein-chlorophyll complex geometry to guide subsequent experimental work and ensure the desired structure can be achieved and validated.

Inventive Principle:
Principle #10Preliminary action

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 designed proteins enable precise control over chlorophyll-chlorophyll distances and orientations, enhancing light harvesting and charge separation efficiency, suitable for energy transfer and conversion technologies.

Implementation Method 1

the polypeptide binds to a chlorophyll (Chl) dimer

Methodology Applied
Scientific EffectNon-covalent binding: Van der Waals Force

Implementation Method 2

Photosynthetic proteins manipulate the distances and angles between chlorophyll (Chl) molecules to tune excitonic coupling and control absorption and fluorescence spectra

Methodology Applied
Scientific EffectLight absorption: Absorption (EM radiation)

Implementation Method 3

Photosynthetic proteins manipulate the distances and angles between chlorophyll (Chl) molecules to tune excitonic coupling and control absorption and fluorescence spectra, excited state dynamics, energy transfer

Methodology Applied
Scientific EffectExcitonic coupling:

Data Source

PatentUS20250326867A1De novo designed chlorophyll special pair proteins
Publication Date: 2025.10.23 UNIV OF WASHINGTON
  • US20250326867A1 patent drawing
  • US20250326867A1 patent drawing
  • US20250326867A1 patent drawing

AI summary

Polypeptides are provide having an amino acid sequence at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the amino acid sequence selected from the group consisting of SEQ ID NO:1-17, wherein the polypeptide binds to a chlorophyll (Chl) dimer, and scaffolds thereof.