Computational Characterization of CNT-Papain Interactions for Developing a Biosensor

Athira, C. R.; Shilpa, S.; Parvathy, C. M.; Nithya, S.; Vinothaa, V.; Subashini, S. P.; Gopal, Kandasamy; Parimalam, Bharath; Namboori, P. K. Krishnan

doi:10.1007/978-3-642-19542-6_108

Cited by 2 publications

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“…Noting the biotechnological and the biomedical applications of papain-like cysteine proteases, traces of those could be found in the environment, pharmaceutical, chemical, and food products, increasing the need to examine different strategies in sensor developments to detect papain-like cysteine proteases. In addition, papain has been further utilized for sensors sensing heavy metal ions [ 20 , 21 ], and bioactive food ingredients [ 22 ], and even proposed as a candidate for the determination of tetrahydrocannabinol derivates in urine [ 23 ]. In those cases, gold nanoparticles were functionalized with papain due to the strong binding between the cysteine thiol group and gold [ 24 ].…”

Section: Introductionmentioning

confidence: 99%

Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development

Marković,

Andrejević,

Milošević

et al. 2023

Biomimetics

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The significant role of papain-like cysteine proteases, including papain, cathepsin L and SARS-CoV-2 PLpro, in biomedicine and biotechnology makes them interesting model systems for sensor development. These enzymes have a free thiol group that is suitable for many sensor designs including strong binding to gold nanoparticles or low-molecular-weight inhibitors. Focusing on the importance of the preservation of native protein structure for inhibitor-binding and molecular-imprinting, which has been applied in some efficient examples of sensor development, the aim of this work was to examine the effects of the free-thiol-group’s reversible blocking on papain denaturation that is the basis of its activity loss and aggregation. To utilize biophysical methods common in protein structural transitions characterization, such as fluorimetry and high-resolution infrared spectroscopy, low-molecular-weight electrophilic thiol blocking reagent S-Methyl methanethiosulfonate (MMTS) was used in solution. MMTS binding led to a two-fold increase in 8-Anilinonaphthalene-1-sulfonic acid fluorescence, indicating increased hydrophobic residue exposure. A more in-depth analysis showed significant transitions on the secondary structure level upon MMTS binding, mostly characterized by the lowered content of α-helices and unordered structures (either for approximately one third), and the increase in aggregation-specific β-sheets (from 25 to 52%) in a dose-dependant manner. The recovery of this inhibited protein showed that reversibility of inhibition is accompanied by reversibility of protein denaturation. Nevertheless, a 100-fold molar excess of the inhibitor led to the incomplete recovery of proteolytic activity, which can be explained by irreversible denaturation. The structural stability of the C-terminal β-sheet rich domain of the papain-like cysteine protease family opens up an interesting possibility to use its foldamers as a strategy for sensor development and other multiple potential applications that rely on the great commercial value of papain-like cysteine proteases.

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Section: Introductionmentioning

confidence: 99%

Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development

Marković,

Andrejević,

Milošević

et al. 2023

Biomimetics

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“…ii) Electrostatic forces include both attractive and repulsive interactions depending on charge carried by the receptor and target. 96,98 Molecules carrying the same charges tend to repel each other while opposite charges exhibit attractive forces. This interaction depends on the electrical charge and the ionic strength of the medium and is nonspecific.…”

Section: 34a Molecular Factorsmentioning

confidence: 99%

Carbon nanotube based electronic detection of biomolecules and chemicals

Krishna¹

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First and foremost, I would like to thank my ex-supervisor, Prof. Zheng Lianxi, for giving me an opportunity to embark on this journey of PhD in the area of nanotechnology. These four years have undoubtedly been the toughest phase of my life as I kept encountering several hurdles both personally and academically. Nevertheless, every time I look up to Prof. Zheng, he has given me priceless suggestions, constant encouragement, and timely guidance, which have largely been the source of my strength during these strenuous phases. Prof. Zheng has been a true role model for me for his simple attitude towards work and life. I am deeply indebted to him, and without his guidance, I would not have been able to improve in various aspects of research and life. I also sincerely thank my current supervisor Prof. Wong Chee How, who has been instrumental in my thesis submission process following Prof. Zheng's departure from NTU. He has been kind and I am extremely grateful to him for lending a helping hand in my troubled times.

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Computational Characterization of CNT-Papain Interactions for Developing a Biosensor

Cited by 2 publications

References 11 publications

Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development

Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development

Carbon nanotube based electronic detection of biomolecules and chemicals

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