MODIFICATION OF SURFACE PLASMON RESONANCE (SPR) BIOSENSOR USING TRANSITION METAL DICHALCOGENIDES MOS2 FOR CFP-10 PROTEIN DETECTION OF MYCOBACTERIUM TUBERCULOSIS
Tuberculosis is a respiratory system disease caused by Mycobacterium tuberculosis (Mtb). Tuberculosis is categorized as a tropical disease and has received special attention from various health institutions because of the high number of sufferers and the harmful effects disease. Handling tubercul...
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Format: | Theses |
Language: | Indonesia |
Online Access: | https://digilib.itb.ac.id/gdl/view/67175 |
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Institution: | Institut Teknologi Bandung |
Language: | Indonesia |
Summary: | Tuberculosis is a respiratory system disease caused by Mycobacterium tuberculosis
(Mtb). Tuberculosis is categorized as a tropical disease and has received special
attention from various health institutions because of the high number of sufferers
and the harmful effects disease. Handling tuberculosis involves multiple strategies,
including developing rapid detection technology. Surface plasmon resonance
(SPR)-based biosensor is a promising detection method because it has real-time
detection features with performance that competes with other conventional
methods. The SPR biosensor can be modified by adding materials on top of Au thin
film, which then functions as a bioreceptor immobilization matrix to increase
surface plasmon activity. Dichalcogenide transition metals are a group of 2D
materials with a large surface area and high optical absorption efficiency. They are
stable and do not interfere with the surrounding biochemical reactions. Therefore,
this material has the potential as a modifier of SPR biosensors that can significantly
improve detection performance.
In this study, the SPR biosensor was modified using one type of transition metal
dichalcogenides material, molybdenum disulfide (MoS2), to detect CFP-10 Mtb
protein. The CFP-10 protein was chosen because it is an early Mtb secretory protein
and is not found in other types of Mycobacterium. MoS2 was synthesized by
hydrothermal method to obtain a flower-like morphology with a small particle size
to provide abundant immobilization sites. MoS2 modification was done by varying
the pH (6, 7, and 8) and the trisodium citrate concentration (0.125; 0.25; 0.5 g).
Trisodium citrate (Na3Ct) is a reducing agent in the synthesis, so it is expected to
reduce the particle size.
Based on XRD results, both pH and Na3Ct affect the diffraction peak's intensity,
indicating the crystallinity of MoS2. Meanwhile, based on the results of SEM, the
effect of pH was not seen significantly, but there was an evident change in particle
size from the variation of Na3Ct. It obtained flower-like MoS2 with the smallest
particle size of ~500 – 600 nm from the synthesis at pH 7 with 0.5 g Na3Ct. The
synthesis product was then used in the SPR test by depositing it on the Au chip with
various deposition cycles (6L, 9L, 12L, and 15L) to see the effect of thickness on
detection performance. The functionalized Au chip with various active groups and
CFP-10 antibody was tested to detect CFP-10 protein with a concentration variation of 62.5; 100; 125; 250; and 500 ng/mL. Each chip shows a detection response in
the form of an increase in unit response change (?RU) as the analyte concentration
increases. Increasing the deposition cycle also increases the sensitivity of the
biosensor on the 6L – 12L chip, but then decreases again on the 15L chip. The best
detection performance resulting from this study was demonstrated by the 12L
Au/MoS2/CFP-10Ab chip with sensitivity and limit-of-detection (LOD) of -1.0059
and 3.45 ng/mL, respectively. Compared to the LOD with the bare Au/CFP-10Ab
chip, which is 7.66 ng/mL, the Au/MoS2/CFP-10Ab 12L provides at least ~45%
better performance. This biosensor also has good selectivity and uniformity based
on testing on various analytes and repeated measurements on 6 different chips.
From this study, it has been proven that MoS2 can significantly improve the
performance of SPR biosensors. Therefore, this Au/MoS2/CFP-10Ab-based SPR
biosensor has the potential to be further developed and applied as a detection
technology for CFP-10 Mtb protein in monitoring and diagnosing tuberculosis.
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