Self-aggregation, Temperature-responsive Agglutination, And pH-induced Disaggregation of Amphiphilic Cyclophane Dimer Having A PEG Linkage

2021 ◽  
Author(s):  
Osamu Hayashida ◽  
Tensho Tomita ◽  
Takaaki Miyazaki
Keyword(s):  
Temperature Responsive ◽  
Aggregation Temperature ◽  
Self Aggregation

Retrieval of resorptive human osteoclasts from temperature-responsive plastic

2016 ◽  
Author(s):  
Arjen Gebraad ◽  
Teuvo Hentunen ◽  
Tiina Laitala-Leinonen
Keyword(s):  
Temperature Responsive ◽  
Human Osteoclasts

Self-Aggregation of Synthetic Protobacteriochlorophyll-d Derivatives

2004 ◽  
Author(s):  
Hitoshi Tamiaki ◽  
Hiroyuki Kitamoto ◽  
Takuya Watanabe ◽  
Reiko Shibata
Keyword(s):  
Self Aggregation

Hsp70 Escort Protein: More Than a Regulator of Mitochondrial Hsp70

2018 ◽  
Vol 16 (1) ◽  
pp. 64-73 ◽  
Author(s):  
David O. Nyakundi ◽  
Stephen J. Bentley ◽  
Aileen Boshoff
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Domain ◽  
C Terminus ◽  
Cellular Localisation ◽  
The Matrix ◽  
Mitochondrial Hsp70 ◽  
Cellular Compartments ◽  
Intramolecular Communication ◽  
Self Aggregation ◽  
J Protein

Hsp70 members occupy a central role in proteostasis and are found in different eukaryotic cellular compartments. The mitochondrial Hsp70/J-protein machinery performs multiple functions vital for the proper functioning of the mitochondria, including forming part of the import motor that transports proteins from the cytosol into the matrix and inner membrane, and subsequently folds these proteins in the mitochondria. However, unlike other Hsp70s, mitochondrial Hsp70 (mtHsp70) has the propensity to self-aggregate, accumulating as insoluble aggregates. The self-aggregation of mtHsp70 is caused by both interdomain and intramolecular communication within the ATPase and linker domains. Since mtHsp70 is unable to fold itself into an active conformation, it requires an Hsp70 escort protein (Hep) to both inhibit self-aggregation and promote the correct folding. Hep1 orthologues are present in the mitochondria of many eukaryotic cells but are absent in prokaryotes. Hep1 proteins are relatively small and contain a highly conserved zinc-finger domain with one tetracysteine motif that is essential for binding zinc ions and maintaining the function and solubility of the protein. The zinc-finger domain lies towards the C-terminus of Hep1 proteins, with very little conservation outside of this domain. Other than maintaining mtHsp70 in a functional state, Hep1 proteins play a variety of other roles in the cell and have been proposed to function as both chaperones and co-chaperones. The cellular localisation and some of the functions are often speculative and are not common to all Hep1 proteins analysed to date.

Aggregation prone regions in antibody sequences raised against Vibrio cholerae: A bioinformatic approach

2020 ◽  
Vol 15 ◽  
Author(s):  
Zakia Akter ◽  
Anamul Haque ◽  
Md. Sabir Hossain ◽  
Firoz Ahmed ◽  
Md Asiful Islam
Keyword(s):  
Vibrio Cholerae ◽  
Binding Sites ◽  
Bioinformatic Analysis ◽  
Antigen Binding ◽  
Short Term ◽  
Protein Database ◽  
The Stability ◽  
Bioinformatic Approach ◽  
Self Aggregation ◽  
Complementarity Determining Region

Background: Cholera, a diarrheal illness causes millions of deaths worldwide due to large outbreaks. Monoclonal antibody used as therapeutic purposes of cholera are prone to be unstable due to various factors including self-aggregation. Objectives: In this bioinformatic analysis, we identified the aggregation prone regions (APRs) of different immunogens of antibody sequences (i.e., CTB, ZnM-CTB, ZnP-CTB, TcpA-CT-CTB, ZnM-TcpA-CT-CTB, ZnP-TcpA-CT-CTB, ZnM-TcpA, ZnP-TcpA, TcpA-CT-TcpA, ZnM-TcpA-CT-TcpA, ZnP-TcpA-CT-TcpA, Ogawa, Inaba and ZnM-Inaba) raised against Vibrio cholerae. Methods: To determine APRs in antibody sequences that were generated after immunizing Vibrio cholerae immunogens on Mus musculus, a total of 94 sequences were downloaded as FASTA format from a protein database and the algorithms such as Tango, Waltz, PASTA 2.0, and AGGRESCAN were followed to analyze probable APRs in all of the sequences. Results: A remarkably high number of regions in the monoclonal antibodies were identified to be APRs which could explain a cause of instability/short term protection of anticholera vaccine. Conclusion: To increase the stability, it would be interesting to eliminate the APR residues from the therapeutic antibodies in a such way that the antigen binding sites or the complementarity determining region loops involved in antigen recognition are not disrupted.

Temperature-modulated cell-separation column using temperature-responsive cationic copolymer hydrogel-modified silica beads

2019 ◽  
Vol 178 ◽  
pp. 253-262 ◽  
Author(s):  
Kenichi Nagase ◽  
Daimu Inanaga ◽  
Daiju Ichikawa ◽  
Aya Mizutani Akimoto ◽  
Yutaka Hattori ◽  
...  
Keyword(s):  
Cell Separation ◽  
Modified Silica ◽  
Copolymer Hydrogel ◽  
Temperature Responsive ◽  
Separation Column ◽  
Silica Beads

Dual pH and temperature responsive hydrogels based on β-cyclodextrin derivatives for atorvastatin delivery

2016 ◽  
Vol 136 ◽  
pp. 300-306 ◽  
Author(s):  
Kaiwen Yang ◽  
Sicheng Wan ◽  
Binbin Chen ◽  
Wenxia Gao ◽  
Jiuxi Chen ◽  
...  
Keyword(s):  
Cyclodextrin Derivatives ◽  
Temperature Responsive ◽  
Responsive Hydrogels
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