Characterization of Stress Responsive Behaviors of Proteins.

Yamahara, Katsuhito; Ota, Hideyuki; Kuboi, Ryoichi

doi:10.1252/jcej.31.795

Cited by 21 publications

(15 citation statements)

References 32 publications

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“…As shown in Fig.4, the LH pr value for seeds of A(1-40) fibrils was very large, even compared with cytochrome c in its molten globular state (LH pr = 2.42) and myoglobin (apo) (LH pr = 2.1). Previously, it has been reported that molten-globule state of proteins showed large LH pr values relative to the native or unfolded state of the proteins [4,14]. The present result suggests that the seeds may act as an intermediate-like species in the fibril formation process similar to the molten-globular (MG) state in the protein (re)folding process.…”

Section: Local Hydrophobicity Of A Fibrils and Their Seedssupporting

confidence: 55%

“…The present result suggests that the seeds may act as an intermediate-like species in the fibril formation process similar to the molten-globular (MG) state in the protein (re)folding process. Since the protein with a large LH pr value is likely to show a large aggregation rate [4], the large LH pr value of seeds implies that the seeds favor aggregation.…”

Section: Local Hydrophobicity Of A Fibrils and Their Seedsmentioning

confidence: 99%

“…Both processes are parallel to the misfolding of proteins and their aggregation process [3], indicating that the interaction between A molecules is a key factor. The hydrophobic interaction is dominant in protein aggregation [4] whereas hydrogen bonding is also the driving force of amyloid fibril formation [5]. However, there are few reports about the above physicochemical property of A.…”

Section: Introductionmentioning

confidence: 99%

“…Alternatively, the aqueous two-phase partitioning (ATPS) method gives the surface net and local hydrophobicity of monomeric or oligomeric proteins such as A [10]. In particular, it has been reported that the local hydrophobicity dominates the aggregation rate of proteins [4]. However, there is a lack of information on the surface properties of intermediates and fibrils required to elucidate the mechanism of amyloid fibril formation.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation

Shimanouchi

Shimauchi

Nishiyama

et al. 2010

SERDJ

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The pathological process of Alzheimer's disease is closely related to amyloid fibril formation by the causative protein, amyloid  (A). The growth behavior of A fibrils is predominated by the seeds-monomeric A interaction. In this study, the local hydrophobicity of seeds of A fibrils was investigated by the aqueous two-phase partitioning method to evaluate the hydrophobic interaction between the seed-monomeric A. The seeds showed a high local hydrophobicity relative to the monomer and fibrils. From the fibril growth experiment and the additive effect of Triton X-100, we could demonstrate the contribution of the hydrophobic seeds-monomer interaction to fibril formation.

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Section: Local Hydrophobicity Of A Fibrils and Their Seedssupporting

confidence: 55%

Section: Local Hydrophobicity Of A Fibrils and Their Seedsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation

Shimanouchi

Shimauchi

Nishiyama

et al. 2010

SERDJ

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“…But, the extreme pH may change protein conformation [39], which might change partitioning of proteins. NaCl is the most common modifying agent of ATP systems for enhancing the hydrophobic protein partitioning into the top phase of PEG-salt systems [38,40,41] or hydrophilic protein partitioning in the bottom phase [42].…”

Section: Effect Of Atp Systems' Parametersmentioning

confidence: 99%

Recovery of Recombinant Proteins from Plants Using Aqueous Two-Phase Partitioning Systems: An Outline

2014

Methods in Molecular Biology

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Transgenic plants producing recombinant proteins are a potential low-cost substitute for complex bioreactors. However, the development of new robust downstream processes to improve protein recovery and isolation from plant feedstock is critical to promote this new technique because downstream processing costs typically contribute to more than 80 % of the total cost. Polishing separation platforms for protein purification, such as chromatography and membrane filtration, have been well established, while little attention has been allocated to initial concentration and separation procedures. In this chapter, application of aqueous two-phase partitioning (ATPP), as an attractive alternative to traditional processes for recovering and isolating target proteins from plant green tissues or seeds, as well as the main advances reported in literature concerning ATPP for the isolation and purification of proteins from plant feedstock are reviewed. The potential application of ATPP as an integrated extraction and isolation step and isolation step after extraction or protein characterization method is discussed separately. The connection of ATPP with traditional protein separation processes is discussed. The separation mechanisms of ATPP are explained based on surface properties of proteins and polymer systems. Finally, the future trends in applying ATPP for protein separation are discussed.

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Evaluation of temperature and guanidine hydrochloride-induced protein–liposome interactions by using immobilized liposome chromatography

Yoshimoto

Shimanouchi

et al. 2006

Biochemical Engineering Journal

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Characterization of Stress Responsive Behaviors of Proteins.

Cited by 21 publications

References 32 publications

Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation

Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation

Recovery of Recombinant Proteins from Plants Using Aqueous Two-Phase Partitioning Systems: An Outline

Evaluation of temperature and guanidine hydrochloride-induced protein–liposome interactions by using immobilized liposome chromatography

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