Abstract
The current work demonstrates the design, characterization, and preparation of molecularly imprinted microspheres for the selective detection of myoglobin in serum samples. The suspension polymerization approach was applied for the preparation of myoglobin imprinted microspheres. For this purpose, N-methacryloylamino folic acid-Nd3+ (MAFol- Nd3+) was chosen as the complex functional monomer. The optimization studies were performed changing the medium pH, temperature, and myoglobin concentration. pH 7.0 was determined as the optimum value where the prepared imprinted microspheres displayed maximum binding for myoglobin. The maximum binding capacity was achieved as 623 mgg−1. In addition, the selectivity studies were conducted. The results confirmed that the imprinted microspheres showed great selectivity towards myoglobin in the existence of hemoglobin, cytochrome c, and lysozyme which were chosen as potentially competing proteins.
Highlights
Myoglobin (Mb) is a hemeprotein which is primarily found in muscle tissues which binds oxygen through its heme functional group
Several conventional approaches such as enzyme-linked immunosorbent assay (ELISA) [14, 15], chromatography [16,17,18,19], electrochemical sensors [20,21,22,23,24], and surface plasmon resonance (SPR) sensors [25,26,27] were applied for the detection of myoglobin
The obtained FT-IR spectra of MIP and nonimprinted microspheres (NIPs) in Figure 2 were similar which confirms that the prepared MIPs and NIPs have similar backbone
Summary
Myoglobin (Mb) is a hemeprotein which is primarily found in muscle tissues which binds oxygen through its heme functional group. The early determination of Mb level is vital for the detection of acute myocardial infarction [6,7,8,9,10,11,12,13] Several conventional approaches such as enzyme-linked immunosorbent assay (ELISA) [14, 15], chromatography [16,17,18,19], electrochemical sensors [20,21,22,23,24], and surface plasmon resonance (SPR) sensors [25,26,27] were applied for the detection of myoglobin. The prepared myoglobin imprinted microspheres were characterized and their binding behaviour towards target protein myoglobin was evaluated
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