thermal aggregation
Recently Published Documents


TOTAL DOCUMENTS

175
(FIVE YEARS 14)

H-INDEX

35
(FIVE YEARS 3)

Biochimie ◽  
2022 ◽  
Author(s):  
Vera A. Borzova ◽  
Natalia A. Chebotareva ◽  
Nikolai N. Sluchanko ◽  
Sergey Yu Kleymenov ◽  
Kira A. Markossian ◽  
...  

2021 ◽  
pp. 129985
Author(s):  
Lu Lu ◽  
Zhen Yang ◽  
Xiao-Na Guo ◽  
Jun-Jie Xing ◽  
Ke-Xue Zhu

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 414
Author(s):  
Sania Bashir ◽  
Ishfaq Ahmad Ahanger ◽  
Anas Shamsi ◽  
Mohamed F. Alajmi ◽  
Afzal Hussain ◽  
...  

Protein aggregation and misfolding are some of the most challenging obstacles, customarily studied for their association with amyloid pathologies. The mechanism of amyloid fibrillation development is a dynamic phenomenon involving various factors such as the intrinsic properties of protein and the physical and chemical environmental conditions. The purpose of this study was to see the thermal aggregation profile of alpha-lactalbumin (α-LA) and to delineate the effect of trehalose on its aggregation profile. α-LA was subjected to thermal aggregation at high concentrations. UV-Vis spectroscopy, a turbidity assay, intrinsic fluorescence, Rayleigh scattering and a thioflavin T (ThT) assay explained the steady outcomes that 1 M trehalose repressed α-LA aggregation in the most effective way followed by 0.75 M and 0.5 M and to a significantly lesser degree by 0.25 M. Multi spectroscopic obser Sania Bashir ations were further entrenched by microscopy. Transmission electron microscopy confirmed that in the presence of its higher concentration, trehalose hinders fibril development in α-LA. In vitro studies were further validated by in silico studies. Molecular docking analysis indicated that trehalose occupied the binding pocket cavity of α-LA and offered several significant interactions, including H-bonds with important residues. This study provides a platform for trehalose in the therapeutic management of protein aggregation-related diseases.


2021 ◽  
Vol 269 ◽  
pp. 106527
Author(s):  
Sushanta Debnath ◽  
Abhijit Chakrabarti

2020 ◽  
Vol 27 (9) ◽  
pp. 2221-2226
Author(s):  
Mohd Shahnawaz Khan ◽  
Shams Tabrez ◽  
Md Tabish Rehman ◽  
Majed S. Alokail

Sign in / Sign up

Export Citation Format

Share Document