Synthesis, Characterization, Interionic Structure, and Self-Aggregation Tendency of Zirconaaziridinium Salts Bearing Long Alkyl Chains

2011 ◽  
Vol 30 (1) ◽  
pp. 100-114 ◽  
Author(s):  
Luca Rocchigiani ◽  
Gianfranco Bellachioma ◽  
Gianluca Ciancaleoni ◽  
Alceo Macchioni ◽  
Daniele Zuccaccia ◽  
...  
Keyword(s):  
Alkyl Chains ◽  
Aggregation Tendency ◽  
Self Aggregation

Self-Aggregation Tendency of All Species Involved in the Catalytic Cycle of Bifunctional Transfer Hydrogenation

2009 ◽  
Vol 28 (4) ◽  
pp. 960-967 ◽  
Author(s):  
Gianluca Ciancaleoni ◽  
Cristiano Zuccaccia ◽  
Daniele Zuccaccia ◽  
Eric Clot ◽  
Alceo Macchioni
Keyword(s):  
Catalytic Cycle ◽  
Transfer Hydrogenation ◽  
Aggregation Tendency ◽  
Self Aggregation

Self-Aggregation Tendency of Zirconocenium Ion Pairs Which Model Polymer-Chain-Carrying Species in Aromatic and Aliphatic Solvents with Low Polarity

2008 ◽  
Vol 14 (22) ◽  
pp. 6589-6592 ◽  
Author(s):  
Luca Rocchigiani ◽  
Cristiano Zuccaccia ◽  
Daniele Zuccaccia ◽  
Alceo Macchioni
Keyword(s):  
Polymer Chain ◽  
Ion Pairs ◽  
Aggregation Tendency ◽  
Self Aggregation

Kinetic studies on the self-aggregation of a non ionic porphyrin in the presence and absence of ionic liquid by molecular dynamics simulation

2012 ◽  
Vol 16 (10) ◽  
pp. 1082-1093 ◽  
Author(s):  
Maryam Ghadamghahi ◽  
Davood Ajloo ◽  
Mahmood Moalem
Keyword(s):  
Molecular Dynamics ◽  
Ionic Liquid ◽  
Molecular Dynamics Simulation ◽  
Kinetic Studies ◽  
Dynamics Simulation ◽  
Alkyl Chains ◽  
Porphyrin Derivative ◽  
Chain Lengths ◽  
Kinetics Of ◽  
Self Aggregation

Aggregation kinetics of a porphyrin derivative in the absence and presence of different concentrations, below and above the critical micelle concentration (CMC) of three ionic liquids (ILs); 1-octyl-3-methylimidazolium, 1-dodecyl-3- methyl imidazolium and 1-octadecyl-3-methylimidazolium chloride was studied using molecular dynamics simulation. Effect of IL, with different chain lengths on the aggregation of a porphyrin derivative, 5,10,15,20-tetrakis(2,5-dihydroxyphenyl)porphyrin, was investigated. The low amount of each ionic liquid (below CMC) observed to favors the formation of aggregates; further increasing ionic liquid concentration leads to the destabilization of aggregates. The compared calculated rate constants also support these results. Aggregation of imidazolium ILs proved to take place with longer alkyl chains that favors aggregation.

PGSE NMR Studies on DAB-Organo-Rhodium Dendrimers:  Evaluation of the Molecular Size, Self-Aggregation Tendency, and Surface Metal Density

2006 ◽  
Vol 25 (9) ◽  
pp. 2201-2208 ◽  
Author(s):  
Daniele Zuccaccia ◽  
Luigi Busetto ◽  
M. Cristina Cassani ◽  
Alceo Macchioni ◽  
Rita Mazzoni
Keyword(s):  
Molecular Size ◽  
Nmr Studies ◽  
Surface Metal ◽  
Pgse Nmr ◽  
Aggregation Tendency ◽  
Self Aggregation

Segmental motion of alkyl chains grafted on silica gel, studied by neutron scattering

1983 ◽  
Vol 44 (4) ◽  
pp. 497-503 ◽  
Author(s):  
J.P. Beaufils ◽  
M. C. Hennion ◽  
R. Rosset
Keyword(s):  
Neutron Scattering ◽  
Silica Gel ◽  
Segmental Motion ◽  
Alkyl Chains

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.

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