Review on some polyphenolic compounds to identify beta amyloid structures among other invitro secondary structures

Sirvan Abbasbeigi,1,*

1. Medical Biology Research Center, University of Medical Sciences, Kermanshah, Iran

Abstract

Introduction

As it was mentioned in our previous report, aurone derivatives originated from polyphenols cluster, and due to its natural features such as neutral load and proper lipophilicity coefficient, there is a good candidate to work on it as a suitable alternative instead of tht compound which may well be known as amyloid plaques probe. we have already argued about protein misfolding disorders, and also it has been described different reasons and nonfunctional pathways which may lead protein to fold improperly in addition to mutation factors. as a result, we have been confronted with so many pathological conditions which they have been linked to protein and protein’s problems. however, in this case, we developed our study to some other aspects of the previous report like antioxidant activities and toxicities plus some newly released data of the last announcement.

Methods

To remind the previous contents, the experiment fundamentally based on purification of proteins and the affinity of synthetic compounds (aurone derivatives) to identify beta structure (extended cross-beta) as accurately as possible among other structures. the proteins which were chosen for this experiment were bovine serum albumin (3v03) as a protein within an alpha/beta combination secondary structure and beta-lactoglobulin (2q2m) as an all beta secondary structure. the process of protein purification (beta-lactoglobulin) was based on fractionation protocol and inducing different ph parameter and also several various temperature degrees. spectroscopic studies have been measured in the each compound’s wavelengths (1-5 compounds) for both uv and fluorescence spectroscopes. furthermore, in this study, we have added antioxidant activates assay in addition to the toxicity of each compounds’ data. in the following, we evaluated docking and the interactions data between amyloid protein and attached compounds regarding the standard probe like tht to promote our study compared with the previous one.

Results

Overall, it has been demonstrated that our synthetic derivates could compete with a benzofuranone compound called tht in somewhere. it means, uv spectroscopy which was done for each compound (1-5) in three different conditions (amyloid, amorphous and native) among five various concentration of each protein illustrated as same as tht result. subsequently, we have been observed and reported in our previous manuscript that compound 4 displayed very similar data compare with a standard probe like tht. moreover, in this new report, we assume that whether compound 4 or 3 which both of them originated from trihydroxy benzofuran structure can play a vital role to detect amyloid aggregation rather than others which were evaluated and also it has been proven by molecular simulation as well.

Conclusion

In conclusion, the previous in-vitro studies have suggested that polyphenolic compounds from food products may be useful in targeting aβ. among all of them, flavonoids have been interested due to their antioxidant, anti-inflammation properties, targeting metal-aβ40 aggregation invitro and diminish cytotoxicity induced by metal-aβ40. recently, it was reported that flavonoids including flavones and aurone serve as a useful molecular probe in the development of imaging agents for β-amyloid plaques in the brain. to explore more helpful candidate for amyloid imaging probes, we selected one of the flavonoids, aurone, as a new core structure.

Keywords

Protein disorders, amyloid aggregation, synthetic compounds, auron derivatives