Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review

Rashid, Md Harun; sen, Priyankar

doi:10.1007/s10930-024-10205-0

Protein J

2024

DOI: 10.1007/s10930-024-10205-0

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Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review

Md Harun Rashid,

Priyankar sen

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2024

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Cited by 2 publications

References 119 publications

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β‐Sheets Orientation in Physisorbed Protein Layers

Piscitelli,

Bajrami,

Franco

et al. 2024

Adv Materials Inter

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Physisorption of antibodies onto surfaces is a low‐cost, rapid, and effective approach for immobilizing bioreceptors in applications such as bioelectronic sensors. However, there is a prevailing notion that physisorbed protein layers lack structural order, thus potentially compromising their stability and sensitivity compared to antibody films that are covalently attached to the substrate surface. This study demonstrates the preferential orientation of β‐sheets within the secondary structure of protein layers, specifically anti‐immunoglobulin G (anti‐IgG) and bovine serum albumin (BSA), when physisorbed onto gold (Au) thin films. Using polarization modulation infrared reflection‐absorption spectroscopy (PM‐IRRAS) and infrared attenuated total reflection (IR‐ATR) spectroscopy, it has been confirmed that the β‐strands in these protein layers are tilted relative to the surface normal by average angles of 75.3° ± 0.4° for anti‐IgG and of 79.3 ± 0.2° for BSA. These results are obtained by analyzing the orientation of the transition dipole moments (TDMs) associated with the amide I molecular vibrations derived from a comparison between experimental and simulated mid‐infrared spectra assuming isotropically oriented TDMs. The simulations incorporate refractive and absorption index dispersions obtained from the IR‐ATR spectra. Thus obtained findings offer valuable molecular‐level insights facilitating the design and optimization of biofunctionalized interfaces in advanced biomedical and biosensing applications.

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β‐Sheets Orientation in Physisorbed Protein Layers

Piscitelli,

Bajrami,

Franco

et al. 2024

Adv Materials Inter

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Exploring the Potential Long-term Impact of SARS-CoV-2 on Protein Misfolding and Amyloid-related Conditions

Rashid,

Singha,

Arshad

et al. 2024

PPL

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The long-term impact of the COVID-19 pandemic concerns risk to human health, particularly its potential association with protein misfolding and amyloidosis. This review article explores the causality relationship between SARS-CoV-2 infection, and protein misfolding, leading to amyloid-related conditions. It delves into the mechanisms by which viral proteins may accelerate amyloid formation, exacerbating post-infection complications, including neurological sequelae. Drawing from interdisciplinary research and clinical observations, the potential links between COVID-19, vaccination, and amyloidosis, emphasize the importance of understanding the longterm effect of post-COVID symptoms. This review examines the potential role of COVID-19-related proteins in the formation of amyloid in other related proteins of amyloidosis.

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Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review

Cited by 2 publications

References 119 publications

β‐Sheets Orientation in Physisorbed Protein Layers

β‐Sheets Orientation in Physisorbed Protein Layers

Exploring the Potential Long-term Impact of SARS-CoV-2 on Protein Misfolding and Amyloid-related Conditions

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