Abstract
We fabricated a simple sensor system for qualitative analysis of glycan-mediated interactions. Our main aim was to establish a ronbbust system that allowes drop-tests without complex fluidics. The test system should be usable in routine analytics in the future and bear sufficient sensitivity to detect binding events in the nanomolar range. For this, we employed optical ring resonators and coated them with high avidity glycopolymers based on N-acetylglucosamine (GlcNAc). These hydrophilic polymers are also very feasible in preventing unspecific protein adsorption. Drop-on binding studies with suitable lectins showed that glycopolymers were specifically recognized by a lectin with GlcNAc-specificity and prevented unspecific protein interactions very well. The system could be elaborated in the future for detection of glycan-mediated interactions in the biomedical field and is promising in means of multiplexed analysis and usage in routine analysis.
Highlights
Lectins are ubiquitous carbohydrate-binding proteins and gain more and more interest in research as they may serve as novel diagnostic disease markers [1,2]
Drop-on binding studies with suitable lectins showed that glycopolymers were recognized by a lectin with glycopolymers based on N-acetylglucosamine (GlcNAc)-specificity and prevented unspecific protein interactions very well
N-acetyl-D-glucosamine (GlcNAc), sodium methoxide (NaOCH3 ), acetyl chloride and silver perchlorate monohydrate (AgClO4 ·H2O) were purchased from Alfa Aesar. 2-hydroxylethyl methacrylate (HEMA), ethyl α-bromoisobutyrate (EBiB) and ammonia were purchased from Merck
Summary
Lectins are ubiquitous carbohydrate-binding proteins and gain more and more interest in research as they may serve as novel diagnostic disease markers [1,2]. Some highly sensitive sensor platforms based on electrochemical approaches [7,8], surface plasmon resonance [9,10], or others are published but suffer so far from laborious production processes, rather complex measuring setups or do not take the tremendous amount of unspecific binding of lectins to surfaces in general into account. In the past we have employed a sensor system, based on glycopolymers as ligands, which showed excellent repellence of unspecific protein adsorption on the one hand, paired with excellent binding efficiency due to the multivalent ligand presentation for lectins on the other [11]. The usage of glycopolymers as specific lectin biosensors is highly advantageous for these systems
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