Structural Change of Apoferritin as the Effect of pH Change: DLS and SANS Study

Patriati, Arum; Suparno, Nadi; Sulungbudi, Grace Tjungirai; Mujamilah, Mujamilah; Putra, Edy Giri Rachman

doi:10.22146/ijc.50630

Cited by 4 publications

(3 citation statements)

References 21 publications

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“…Small angle neutron/X-ray scattering (SANS or SAXS) technique has been widely used in protein structure determination. The information of globular structure of protein, the conformational change of protein, the dimerization of protein, and the aggregation of protein has been revealed by SAXS [14,15]. The advancement of this techniques is relied on its ability to reveal the protein structure in solution and its possibility to undergo in-situ experiment [16].…”

Section: Introductionmentioning

confidence: 99%

The Influence of Zinc Ions in Insulin Fibrillation by Heat at Acid Solution Revealed Using Small Angle X-Ray Scattering

Patriati¹,

Suparno²,

Soontaranon

et al. 2021

KEM

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The fibrillation mechanism of insulin in acid solution has been studied by small angle X-ray scattering (SAXS). It was observed that insulin monomer unfolded in both conditions. Furthermore, in zinc free solution, insulin tend to aggregate on heating start in the first 5 min. The fibrillation through aggregation process continues until 30 min on heating. The similar phenomenon occurs in the presence of zinc ions. The SAXS data suggest that the presence of zinc ions prevent the long cylindrical fibril at the beginning of heating. However, after 20 min heating, the large cylindrical fibril of insulin formed in both conditions.

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Section: Introductionmentioning

confidence: 99%

The Influence of Zinc Ions in Insulin Fibrillation by Heat at Acid Solution Revealed Using Small Angle X-Ray Scattering

Patriati¹,

Suparno²,

Soontaranon

et al. 2021

KEM

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“…Small angle neutron scattering (SANS) is considered as a powerful tool to overcome that limitation which can provide low resolution of threedimensional structural information of macromolecules in solution [10]. Although SANS is a low resolution method, this technique allows to study native protein structures in near physiological conditions and analysis of its structural changes [11]. Here, the structures of BSA in solution were investigated by SANS technique.…”

Section: Introductionmentioning

confidence: 99%

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

Patriati

Putra

2021

Jurnal Teknologi

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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.

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“…However, only small angle scattering technique, both SANS and SAXS, that can give the information of the BSA shape and size in solution. Small angle scattering is a powerful tool to study protein structure in solution [10]- [12]. Furthermore, as the best of our knowledge, the study of the conformational change due to the denaturation of a high concentration BSA as the addition of SDS have not been reported yet.…”

Section: Introductionmentioning

confidence: 99%

Sans Studies on the Bovine Serum Albumin Denaturation in the Presence of SDS

Rahayu

Patriati

Suparno

et al. 2021

jsmi

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The effect of the presence of sodium dodecyl sulfate (SDS) on the denaturation of bovine serum albumin (BSA) has been studied using 36 m small-angle neutron scattering (SANS) BATAN spectrometer (SMARTer). The neutron scattering data reduction used the Graphical Reduction and Analysis SANS Program (GRASP) software, and the fitting process used the IGOR SANS Analysis software. The denaturation process was identified by observing the changes BSA globular structure. The experimental results showed the addition of SDS at low concentrations (2 mM, 5 mM, 10 mM) into BSA solution at pH 7 do not cause a significant change in the size of the BSA globular structure. The SANS scattering profile of BSA fitted with the triaxial ellipsoid model, a simple shape approach for protein globular structure. The fitting result showed the semi-axis B for BSA in the addition of 2 mM, 5 mM, 10 mM SDS were 33.8 Å, 33.8 Å, and 37.8 Å, respectively. While the semi-axis A and semi-axis C were constant for those three variations at 14.6 Å and 32.2 Å, respectively. In higher addition of SDS, the globular structure of BSA unfolded into flexible cylinder structure with the radius of 14.4 Å and length of 83.5 Å. The denaturation of BSA was clearly showed by the addition of 40 mM SDS. The structure of BSA in this condition fitted to fractal structure with fractal dimension of 1.1, the block radius of 16.7 Å and the correlation length of 42.5 Å. These results indicated that the addition of SDS at low concentrations has not caused the denaturation of BSA. Meanwhile, the addition of SDS at high concentrations made BSA to unfold that lead to the denaturation of BSA.

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Structural Change of Apoferritin as the Effect of pH Change: DLS and SANS Study

Cited by 4 publications

References 21 publications

The Influence of Zinc Ions in Insulin Fibrillation by Heat at Acid Solution Revealed Using Small Angle X-Ray Scattering

The Influence of Zinc Ions in Insulin Fibrillation by Heat at Acid Solution Revealed Using Small Angle X-Ray Scattering

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

Sans Studies on the Bovine Serum Albumin Denaturation in the Presence of SDS

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