Abstract
Signature-based protein sensing has recently emerged as a promising prospective alternative to conventional lock-and-key methods. However, most of the current examples require the measurement of optical signals from spatially-separated materials for the generation of signatures. Herein, we present a new approach for the construction of multi-fluorescent sensing systems with high accessibility and tunability, which allows generating protein fluorescent signatures from a single microplate well. This approach is based on conjugates between nano-graphene oxide (nGO) and three single-stranded DNAs (ssDNAs) that exhibit different sequences and fluorophores. Initially, the three fluorophore-modified ssDNAs were quenched simultaneously by binding to nGO. Subsequent addition of analyte proteins caused a partial recovery in fluorescent intensity of the individual ssDNAs. Based on this scheme, we have succeeded in acquiring fluorescence signatures unique to (i) ten proteins that differ with respect to pI and molecular weight and (ii) biochemical marker proteins in the presence of interferent human serum. Pattern-recognition methods demonstrated high levels of discrimination for this system. The high discriminatory power and simple format of this sensor system should enable an easy and fast evaluation of proteins and protein mixtures.
Highlights
The accurate identification of proteins is of critical importance for the understanding of a variety of biological processes and diseases [1,2]
These single-stranded DNAs (ssDNAs) bear different sequences, and two of these can fold into different higher-order structures, which were expected to impart the individual elements of the sensor system with differential cross-reactivity [38,39]
We have developed a multi-fluorescent ssDNAs/nano-graphene oxide (nGO) sensor for the discrimination of proteins
Summary
The accurate identification of proteins is of critical importance for the understanding of a variety of biological processes and diseases [1,2]. Signature-based sensing has emerged as a promising prospective alternative to lock-and-key specific recognition [4,5]. A subsequent pattern-recognition of the -obtained signatures enables the accurate identification of proteins. Signature-based sensing has been successfully employed for the detection of proteins in dilute solutions [6,7,8,9,10,11,12,13,14,15,16,17] and in biological matrices [18,19,20,21,22,23,24,25,26,27]. Most of the current examples require the measurement of optical signals from spatially-separated materials for the generation of signatures, e.g., in multiple wells of a microplate, which significantly limits the scope for applications that depend on a simple and rapid identification of proteins
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