scholarly journals Conditions of the Oligomer Formation of VTES and VTMS Suitable for the Donation of Effective Hydrophobicity to TiO2.

2002 ◽  
Vol 53 (4) ◽  
pp. 273-277 ◽  
Author(s):  
Sumiko SANUKI ◽  
Yoshihiko NISHI ◽  
Toshihiro YOSHIMOTO ◽  
Hiroshi MAJIMA
Keyword(s):  
Oligomer Formation

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.

scholarly journals Hsp70 chaperone blocks α-synuclein oligomer formation via a novel engagement mechanism

2021 ◽  
Vol 296 ◽  
pp. 100613
Author(s):  
Jiahui Tao ◽  
Amandine Berthet ◽  
Y. Rose Citron ◽  
Paraskevi L. Tsiolaki ◽  
Robert Stanley ◽  
...  
Keyword(s):  
Oligomer Formation ◽  
Hsp70 Chaperone

Dynamics of oligomer formation by denatured carbonic anhydrase II

2008 ◽  
Vol 1784 (5) ◽  
pp. 834-842 ◽  
Author(s):  
Dmitry A. Prokhorov ◽  
Alexander A. Timchenko ◽  
Vladimir N. Uversky ◽  
Vladimir S. Khristoforov ◽  
Hiroshi Kihara ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Oligomer Formation

scholarly journals Biocompatible and blood–brain barrier permeable carbon dots for inhibition of Aβ fibrillation and toxicity, and BACE1 activity

Nanoscale ◽  
2017 ◽  
Vol 9 (35) ◽  
pp. 12862-12866 ◽  
Author(s):  
Xu Han ◽  
Zhifeng Jing ◽  
Wei Wu ◽  
Bing Zou ◽  
Zhili Peng ◽  
...  
Keyword(s):  
Blood Brain Barrier ◽  
Carbon Dots ◽  
Brain Barrier ◽  
Oligomer Formation ◽  
Blood Brain ◽  
Bace1 Activity ◽  
Toxic Oligomer

The blood–brain barrier permeable C-Dots can deactivate the BACE1 and further inhibit Aβ fibrillation and toxic oligomer formation.

scholarly journals Binding Component of Clostridium perfringens Iota-Toxin Induces Endocytosis in Vero Cells

2002 ◽  
Vol 70 (4) ◽  
pp. 1909-1914 ◽  
Author(s):  
Masahiro Nagahama ◽  
Koichi Nagayasu ◽  
Keiko Kobayashi ◽  
Jun Sakurai
Keyword(s):  
Clostridium Perfringens ◽  
Vero Cells ◽  
Binary Toxin ◽  
Wild Type ◽  
Oligomer Formation ◽  
Clostridium Perfringens Iota Toxin ◽  
Binding Component ◽  
Pronase Treatment

ABSTRACT Clostridium perfringens iota-toxin is a binary toxin consisting of two individual proteins, the binding component (Ib) and the enzyme component (Ia). Wild-type Ib bound to Vero cells at 4 and 37°C and formed oligomers at 37°C but not at 4°C. The Ib-induced K+ release from the cells was dependent on the oligomer formation of Ib in the cells, but the oligomer formation did not induce rounding activity or cytotoxicity. After incubation of the cells with recombinant Ib (rIb) at 37°C, the Ib oligomer in the cell became resistant to pronase treatment with time, but the Ib monomer was sensitive to the treatment. Furthermore, treatment of Vero cells with rIb in the presence of bafilomycin, methylamine, or ethylamine resulted in accumulation of the oligomer in the cells but had no effect on K+ release. Moreover, incubation with Ib plus Ia in the presence of these agents caused no rounding in the cells. These observations suggest that Ib binds to Vero cells, itself oligomerizing to form ion-permeable channels and that the formation of oligomer then induces endocytosis.

Abstract 626: Interaction Between The Ang-(1-7) Receptor Mas And The Bradykinin B2 Receptor: Functional Implications

Hypertension ◽  
2014 ◽  
Vol 64 (suppl_1) ◽  
Author(s):  
Bruno Cerrato ◽  
Oscar Carretero ◽  
Hernán Grecco ◽  
Mariela M Gironacci
Keyword(s):  
Plasma Membrane ◽  
Binding Assays ◽  
Transfected Cells ◽  
Oligomer Formation ◽  
Early Endosomes ◽  
Functional Implications ◽  
Functional Consequences ◽  
Ligand Stimulation ◽  
G Protein Coupled ◽  
Fluorescence Energy

G protein-coupled receptors (R) exist as homo- or hetero-oligomers, which is essential for receptor function. Since BK actions were blocked by a Mas R antagonist or that Ang-(1-7) responses disappeared when the BK receptor B2 was blocked, we hypothesized that Mas and B2 Rs on the plasma membrane may interact through hetero-oligomer formation. Our aim was to investigate the existence of heteromerization between Mas and B2 Rs by the fluorescence energy transfer (FRET) technique and the functional consequences of this oligomer formation. HEK293T cells were transfected with the coding sequence for Mas R fused to YFP and B2 R fused to CFP. After 48 h cells were incubated in the absence and presence of 1 μM Ang-(1-7) or BK during 15 min and interaction between Mas and B2 R was evaluated by FRET. Functional consequences of this interaction were determined by ligand binding assays. A positive FRET was observed in cells cotransfected with MasR-YFP and B2R-CFP, suggesting that both Mas and B2 Rs interact by a hetero-oligomer formation in a constitutive manner. This hetero-oligomer was not altered by the agonist because FRET was not modified when the cells were stimulated with BK or Ang-(1-7). Ang-(1-7) or BK induced internalization of this hetero-oligomer into early endosomes since MasR-YFP or B2R-CFP colocalized with Rab-5, an early endosome marker, after ligand stimulation. When MasR-YFP plus B2R-CFP transfected cells were stimulated with Ang-(1-7) there was a decrease of 82±6% in Mas R and 58±4% in B2 R present in the plasma membrane. Conversely, when MasR-YFP plus B2R-CFP transfected cells were stimulated with BK there was a decrease of 91±4% in B2 R and 53±3% in Mas R in the plasma membrane. This result clearly demonstrates that in co-expressing cells of both receptors the selective stimulation of one of the GPCRs promotes co-internalization of both receptors. We conclude that Mas and B2 Rs constitutively interact through an hetero-oligomer formation at the plasma membrane which may explain the cross-talk between Ang-(1-7) and BK. This hetero-oligomer is internalized upon stimulation with either Ang-(1-7) or BK, leading to a decrease in the number of Rs present in the membrane.

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