Polydispersity as a Parameter for Indicating the Thermal Stability of Proteins by Dynamic Light Scattering

Shiba, Kohei; Niidome, Takuro; Katoh, Etsuko; Xiang, Hongyu; Han, Lu; Mori, Takeshi; Katayama, Yoshiki

doi:10.2116/analsci.26.659

Cited by 44 publications

(27 citation statements)

References 49 publications

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“…Because of recent improvements in instrument sensitivity, even proteins that produce weak light scattering intensity can be studied using DLS measurements [13][14]. Furthermore, the polydispersity obtained from DLS measurement is often used as a parameter for predicting protein crystal formation [15][16], indicating that DLS measurements can be adapted to study amyloid fibril formation.…”

Section: Introductionmentioning

confidence: 99%

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Saiki

Shiba²,

Okumura

2015

FEBS Letters

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a b s t r a c tAmyloid fibrils are fibrous protein assemblies with distinctive cross-b structures. For amyloidosis, there are disease-associated mutations outside of the cross-b structures. Thus, it is necessary to elucidate the role of peripheral sequences outside the cross-b structure. Amyloid fibrils are generally 10 nm in width; however, the amyloid fibrils of truncated barnase M1 peptides missing the Cterminal sequence outside the cross-b structure are 20 nm in width. In this study, we performed comparative analysis of the structural stability of amyloids formed by the respective peptides. We found that the C-terminal amino acids dramatically affect the conformational instability in the presence of a denaturing reagent.

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Section: Introductionmentioning

confidence: 99%

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Saiki

Shiba²,

Okumura

2015

FEBS Letters

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“…The hydrodynamic parameters obtained from DLS measurement are useful for predicting the stability of proteins and their functions [31]. The hydrodynamic diameter and polydispersity of L-CD conjugates are slightly higher than those for unmodified protein (Fig.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of β-cyclodextrin-lysozyme conjugates and their physicochemical and biochemical properties

Goszczyński

Gawłowski

Girek

et al. 2017

J Incl Phenom Macrocycl Chem

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Recently a great interest in the field of protein engineering and the design of innovative drug delivery systems employing specific ligands such as cyclodextrins is observed. The paper reports the solid state, thermal method for protein coupling with β-cyclodextrin and the physicochemical and biological properties of the obtained conjugates. The structure of the obtained conjugates was investigated via liquid chromatography-mass spectrometry, dynamic light scattering and circular dichroism analysis. The presented conjugates were biologically active and covalently bound β-cyclodextrin preserved the ability to form inclusion complexes with the model compound. This report demonstrates the great potential of cyclodextrin as a modifying unit that can be used to modulate the properties of therapeutic proteins, additionally giving such conjugates the possibility to transport many therapeutic substances in the form of inclusion complexes. In addition, the paper presents the potential of protein-cyclodextrin conjugates to construct innovative bioactive molecules for biological and medical applications.Electronic supplementary materialThe online version of this article (doi:10.1007/s10847-017-0706-8) contains supplementary material, which is available to authorized users.

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“…The experiment was to measure the hydrodynamic radius of the KinB-SD and its evolution during a heating ramp in the presence and absence of small ligands. An increase of the hydrodynamic radius of a protein with a temperature is an indication of protein thermal denaturation and subsequent aggregation (45). A shift of the temperature in the presence of a potential ligand suggests an influence of the ligand on the thermal stability/ unfolding/aggregation of the protein.…”

Section: Methodsmentioning

confidence: 99%

Sensor Domain of Histidine Kinase KinB of Pseudomonas

Tan

Chhor

Binkowski

et al. 2014

Journal of Biological Chemistry

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Background:The sensor domain (SD) of histidine kinase (HK) KinB (KinB-SD) receives signals from the environment and induces a transduction cascade. Results: Structures of the KinB-SD were obtained in ligand-free, phosphate-bound, and mutant forms. Conclusion:The unique helix-swapped KinB-SD structure forms a ligand-binding cavity on the dimer interface. Significance: KinB-SD studies provide insights into the signal transduction and identity of potential signaling molecules.

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Polydispersity as a Parameter for Indicating the Thermal Stability of Proteins by Dynamic Light Scattering

Cited by 44 publications

References 49 publications

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Synthesis of β-cyclodextrin-lysozyme conjugates and their physicochemical and biochemical properties

Sensor Domain of Histidine Kinase KinB of Pseudomonas

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