A Comprehensive Review of the Aggregated Proteins through Routine Optical Studies Aiming to be Replaced by Aurone-specific Derivatives

Students often recognize biochemistry as a research-oriented system. It is effortless to see the spread of this view because everyday students pay more attention to what their instructors concentrate on and witness professors’ basic research in the laboratory. Meanwhile, biochemistry science depends on research activities that are fundamental and theoretical but always alongside very practical or applied aspects as well. In amyloid studies nearly 30 years ago, many probes have emerged exhibiting various responses to amyloids, such as intensity changes, shifts in fluorescence maxima, and variations in lifetimes, among many others. These probes have shed light on various topics, including the kinetics of amyloid aggregation, the effectiveness of amyloid aggregation inhibitors, the elucidation of binding sites in amyloid structures, and the staining of amyloid aggregates in vitro, ex vivo, and in vivo. Therefore, this study is considered one of the most debatable subjects currently being used in different investigations. This review is based on published studies associated with aggregated protein probes and detectors (whether synthetic or intrinsic). It has also tried to cover the common concern introducing the most applicable ones In vitro/vivo. Furthermore, this glance looks into several well-known chemical and biochemical methods to follow protein aggregation assembly compared with lately used protocols. Interestingly, the provided content does not intend to prioritize intrinsic or synthetic staining methods but also attempts to illustrate a parallel pathway and ultimately express an expanded point of view.