ICAM-1 Aptamer Structure for Blocking Rhinovirus Attachment

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Solution Overview

Problem

There is a need for aptamers that selectively bind to cellular membrane glycoproteins, particularly ICAM-1, to prevent human rhinovirus binding and infection, as current treatments lack effective antiviral drugs for common colds caused by rhinoviruses.

Innovation Solution

Development of nucleic acid aptamers with high binding affinity and specificity for ICAM-1, configured to inhibit human rhinovirus binding through a secondary structure comprising a stem, hairpin loop, and dangling ends, using SELEX technology to select aptamers that reduce virus attachment to cellular receptors.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If aptamers are designed to bind to ICAM-1 with high affinity and specificity, then viral binding is inhibited, but the complexity of aptamer structure increases

Engineering Contradiction:

Improvebinding affinity and specificityVSAvoidaptamer structure complexity

Core Design Contradiction:

ReliabilityVSDevice complexity

Solution Approach 1:

The aptamer is divided into functional segments: a binding region that specifically recognizes ICAM-1 and terminal regions (5' and 3' ends) that form stable secondary structures. This segmentation allows the binding region to optimize affinity for ICAM-1 while the terminal regions provide structural stability without interfering with binding specificity.

Inventive Principle:

Principle #1Segmentation

Solution Approach 2:

The aptamer employs dynamic secondary structures (hairpin loops and dangling ends) that can adapt their conformation. The hairpin loops provide structural stability while remaining flexible enough to allow the binding region to properly interact with ICAM-1, balancing structural complexity with functional effectiveness.

Inventive Principle:

Principle #15Dynamics

2Stability of the object's composition

If aptamers use complex secondary structures (stem, hairpin loop, dangling ends), then binding stability improves, but manufacturing complexity increases

Engineering Contradiction:

Improvebinding stabilityVSAvoidaptamer synthesis complexity

Core Design Contradiction:

Stability of the object's compositionVSEase of manufacture

Solution Approach 1:

The aptamer sequence is designed to self-fold into the required secondary structures through intrinsic base pairing. The 5' and 3' terminal regions automatically form hairpin loops and dangling ends when the aptamer is synthesized, eliminating the need for post-synthesis structural assembly or complex manufacturing processes. The sequence itself encodes the structural information needed for stable folding.

Inventive Principle:

Principle #25Self-service

3Ease of manufacture

If aptamers are truncated to reduce complexity, then manufacturing becomes easier, but binding affinity may be reduced

Engineering Contradiction:

Improveaptamer synthesis simplicityVSAvoidbinding affinity

Core Design Contradiction:

Ease of manufactureVSReliability

Solution Approach 1:

The invention extracts and retains only the essential functional elements: a minimized binding region that maintains ICAM-1 specificity and necessary terminal sequences for secondary structure formation. Non-essential sequences are removed through truncation, achieving the optimal balance between manufacturing simplicity and binding affinity. The binding region is precisely defined to include only the nucleotides necessary for ICAM-1 recognition.

Inventive Principle:

Principle #2Taking out (Extraction)

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 aptamers effectively inhibit human rhinovirus binding to ICAM-1, potentially reducing the incidence and severity of common cold symptoms by mitigating viral entry into nasal and throat cells.

Implementation Method 1

The molecular recognition of aptamers is based on structure compatibility and intermolecular interactions

Methodology Applied

Scientific EffectMolecular recognition:

Implementation Method 2

including electrostatic forces, van der Waals interactions, hydrogen bonding, and π-π stacking interactions

Methodology Applied

Scientific EffectElectrostatic forces:

Implementation Method 3

including electrostatic forces, van der Waals interactions, hydrogen bonding, and π-π stacking interactions

Methodology Applied

Scientific Effectvan der Waals interactions: Van der Waals Force

Implementation Method 4

including electrostatic forces, van der Waals interactions, hydrogen bonding, and π-π stacking interactions

Methodology Applied

Scientific EffectHydrogen bonding:

Implementation Method 5

including electrostatic forces, van der Waals interactions, hydrogen bonding, and π-π stacking interactions

Methodology Applied

Scientific Effectπ-π stacking interactions:

Data Source

PatentUS12584137B2Aptamers for personal health care applications

Publication Date: 2026.03.24 CO THE P&G COMP

AI summary

An aptamer composition is disclosed which has one or more oligonucleotides that include at least one of deoxyribonucleotides, ribonucleotides, derivatives of deoxyribonucleotides, derivatives of ribonucleotides, or mixtures thereof. The aptamer composition has a binding affinity for one or more cellular membrane glycoproteins selected from the group consisting of: intercellular adhesion molecule 1 (ICAM-1), low-density lipoprotein receptor (LDLR) family members, and cadherin-related family member 3 (CDHR3), preferably intercellular adhesion molecule 1 (ICAM-1), and is configured to reduce the binding of one or more human rhinoviruses to the intercellular adhesion molecule 1 (ICAM-1).