Interaction of bovine serum albumin (BSA) protein with mixed anionic-cationic surfactants and resultant structure

Soft Matter ◽  
2021 ◽  
Author(s):  
Debasish Saha ◽  
Debes Ray ◽  
Sugam Kumar ◽  
Joachim Kohlbrecher ◽  
Vinod Kumar Aswal
Keyword(s):  
Bovine Serum Albumin ◽  
Sodium Dodecyl Sulfate ◽  
Serum Albumin ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Cationic Surfactants ◽  
Small Angle Neutron Scattering ◽  
Sodium Dodecyl ◽  
Dodecyltrimethylammonium Bromide

The interaction of bovine serum albumin (BSA) protein with the mixture of anionic sodium dodecyl sulfate (SDS) and cationic dodecyltrimethylammonium bromide (DTAB) has been investigated by small-angle neutron scattering (SANS)...

Effect of urea on heat-induced gelation of bovine serum albumin (BSA) studied by rheology and small angle neutron scattering (SANS)

2017 ◽  
Vol 29 (2) ◽  
pp. 101-113 ◽  
Author(s):  
Osita Sunday Nnyigide ◽  
Yuna Oh ◽  
Hyeong Yong Song ◽  
Eun-kyoung Park ◽  
Soo-Hyung Choi ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Small Angle Neutron Scattering

scholarly journals pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

2021 ◽  
Vol 83 (2) ◽  
pp. 117-123
Author(s):  
Arum Patriati ◽  
Edy Giri Rachman Putra
Keyword(s):  
Crystal Structure ◽  
Protein Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Small Angle Neutron Scattering ◽  
Static State ◽  
Ph Dependent

The pH-dependent structures of the bovine serum albumin (BSA), under physiological conditions that permit enzymatic activity, were investigated by small-angle neutron scattering (SANS). The unfolding behavior of BSA in solution is important to understand the mechanism of protein aggregation due to protein conformational change. The information of protein structure is crucial to design the perfect protein-based drug delivery device. This information will be useful as a complementary data of BSA crystal structure in static state. The structure of BSA in solution was found to be heart shaped, nearly identical to bovine serum albumin crystal structure. The globular heart shaped structure of BSA was still maintained at alkaline pH range of 7 to 11. It underwent partial unfolding at pH 5 and continued to unfold at pH 3. The unfolded-structure of BSA shows that the globular structure started to change into a cylinder-like structure at pH 3 which was clearly shown in Kratky plot. These results were confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIF in obtaining the three-dimensional protein structure model.

scholarly journals Dynamic Measurements of Bovine Serum Albumin Aggregation Using Small Angle Neutron Scattering

2018 ◽  
Author(s):  
James I Austerberry ◽  
Daniel J Belton
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Aggregation ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Small Angle Neutron Scattering ◽  
Scattering Data ◽  
Complex Nature ◽  
Population Modelling

AbstractThe rapid and complex nature of protein aggregation makes the identification of aggregation mechanisms and their precursors challenging. Here we demonstrate the novel use of small-angle neutron scattering to perform dynamic real-time measurement and analysis of protein aggregation. Changes in bovine serum albumin monomer population and aggregate size are identified at several isothermal temperatures. Kratky plots indicate that the aggregation of BSA occurs through the partial unfolding of the monomer. Dual population modelling of the scattering data indicates that the protein nucleates and grows through a two stage mechanism; a rapid burst phase and a slower growth phase. Both stages are observed to follow Arrhenius behaviour between 70-80 °C.

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