International Biological and Biomedical Journal
IBBJ
Medical Sciences
http://ibbj.org
1
admin
2423-4478
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7
14
2423
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en
jalali
1399
7
1
gregorian
2020
10
1
6
3
online
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fulltext
en
Investigation the protective ability of Pulicaria. undulata aqueous extract on aggregation of κ -casein
Clinical Biochemistry
Clinical Biochemistry
Original Article
Original Article
Protein aggregation is phenomenon wherein protein loses its native structure and aggregates due to the adaption of non-native conformation. Amyloid aggregation formed by the accumulation of various proteins causes many diseases in humans and other organisms. Antioxidants can prevent proteins aggregation. <em>Pulicaria undulata </em> extract along with phenolic compounds can increase protein stability and prevent the aggregation of proteins. The aim of this study is to investigate the aggregation of reduced κ-casein in the presence and absence of <em>P.undulata</em> extract. Interaction between the extract and the κ-casein was investigated by Thioflavin T fluorescence, intrinsic fluorescence intensity, 1-Anilino-8-naphthalene sulfonic acid( ANS) binding assay and circular dichroism (CD) spectroscopy. The result of ThT binding assay indicated that the increase fluorescence intensity of 1,4- dithiothreithol(DTT)-reduced κ-casein is a result of amyloid fibril formation increased in the presence of different concentrations of <em>P.undulata </em>extract in the lag phase. This indicates that <em>P.undulata </em>extract reduces amyloid formation. And fluorescence test of reduced κ-casein indicates a high fluorescence intensity in the absence of <em>P.undulata </em>extract , and the fluorescence decreases when smallest amount of <em>P.undulata </em>extract was used. Using a fluorescence study of far-CD spectrum of κ-casein in the presence and absence of <em>P.undulata </em>extract<em> </em>revealed that the extract prevents changes in secondary structure in the protein. <em>P.undulata</em> extract interacts with the hydrophobic region of κ-casein and prevents hydrophobic-hydrophobic protein interaction and therefore protein aggregation. <span dir="RTL"></span>
P.undulata, κ-casein, aggregation
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http://ibbj.org/browse.php?a_code=A-10-369-1&slc_lang=en&sid=1
Haniyeh
Hashemi pour
hanieh_hashemi66@yahoo.com
10031947532846003854
10031947532846003854
Yes