Fluorescent Saccharide Substrates for Near-Infrared Enzymatic Detection
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Solution Overview
Problem
Current fluorescent enzymatic substrates of saccharide nature lack fluorophores that absorb and emit in the near infrared range, limiting their use for in vivo enzymatic activity detection due to incomplete fluorescence inhibition and reduced detection sensitivity.
Innovation Solution
A fluorescent enzymatic substrate with a fluorophore and an inhibitor attached to the same saccharide unit, allowing for broader fluorophore choices, enhanced sensitivity, and improved solubility, particularly using fluorophores that emit in the near infrared range.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If fluorophores are attached to saccharide substrates for enzymatic detection, then detection sensitivity is improved, but fluorescence inhibition becomes incomplete leading to reduced detection precision
Solution Approach 1:
The patent introduces a specific chemical structure as an intermediary between the fluorophore and saccharide unit that enables complete fluorescence inhibition. This intermediary structure acts as a mediator that, when positioned between the fluorophore and enzyme substrate, ensures total quenching of fluorescence in the intact substrate while allowing complete restoration of fluorescence upon enzymatic cleavage, thereby resolving the contradiction between detection sensitivity and inhibition completeness
Solution Approach 2:
The patent applies local quality by creating a specific functional region in the molecule where the fluorophore is attached to the saccharide unit through a controlled chemical linkage. This localized structural arrangement ensures that fluorescence inhibition occurs specifically at the fluorophore-saccharide interface while maintaining the enzymatic substrate's overall structure and reactivity, enabling precise control over fluorescence behavior without compromising enzymatic function
2Measurement precision
If fluorophores absorbing and emitting in near infrared range are used for in vivo imaging, then detection sensitivity is improved, but fluorescence inhibition becomes incomplete reducing measurement precision
Solution Approach 1:
The patent introduces a specific chemical structure as an intermediary between the fluorophore and saccharide unit that enables complete fluorescence inhibition. This intermediary structure acts as a mediator that, when positioned between the fluorophore and enzyme substrate, ensures total quenching of fluorescence in the intact substrate while allowing complete restoration of fluorescence upon enzymatic cleavage, thereby resolving the contradiction between detection sensitivity and inhibition completeness
Solution Approach 2:
The patent applies parameter changes by optimizing the chemical and physical properties of the linkage between the near-infrared fluorophore and the saccharide unit. By adjusting parameters such as the chemical structure, length, and composition of this linkage, the patent achieves complete fluorescence inhibition specifically for near-infrared emitting fluorophores, enabling their use in in vivo imaging without compromising measurement precision
3Adaptability or versatility
If fluorophore choices are expanded to include near infrared emitting fluorophores, then adaptability is improved, but fluorescence inhibition completeness deteriorates
Solution Approach 1:
The patent applies universality by designing a fluorophore-saccharide linkage system that functions universally across different fluorophore types, including visible and near-infrared emitting fluorophores. This universal linkage structure maintains the ability to provide complete fluorescence inhibition regardless of the specific fluorophore's emission wavelength, thereby enabling broad adaptability without compromising inhibition completeness
Solution Approach 2:
The patent introduces a specific chemical structure as an intermediary between the fluorophore and saccharide unit that enables complete fluorescence inhibition. This intermediary structure acts as a mediator that, when positioned between the fluorophore and enzyme substrate, ensures total quenching of fluorescence in the intact substrate while allowing complete restoration of fluorescence upon enzymatic cleavage, thereby resolving the contradiction between detection sensitivity and inhibition completeness
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
This configuration increases detection sensitivity and facilitates in vivo imaging by providing effective fluorescence inhibition and improved signal acquisition conditions, enabling more efficient enzymatic activity detection.
Implementation Method 1
fluorescent enzymatic substrates of saccharide nature comprising, on the same saccharide unit, a fluorophore F1 and an inhibitor of the fluorescence of F1
Implementation Method 2
substrates for detecting β-gal and β-glu enzymatic activities
Data Source
AI summary
A fluorescent enzymatic substrate including a backbone saccharide nature having at least one saccharide unit. The saccharide unit includes a fluorophore F1 and an inhibitor I1 of the fluorescence of F1. The fluorophore F1 and the inhibitor I1, either directly or by the spacer arms B1 and B2, respectively, when at least one B1 and B2 is present, are grafted on the same saccharide unit of the backbone saccharide. One of th groups is F1 and I1 grafted in the anomeric position 1 of the saccharide unit.