Combining Self-Aggregation Vector and Indicator Matrix for Improved Object Retrieval

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.

Download Full-text

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

Current Bioinformatics ◽

10.2174/1574893615666200106120504 ◽

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.

Download Full-text

Towards a molecular understanding of cation‐anion interactions and self‐aggregation of adeninate salts in DMSO by NMR and UV spectroscopy and crystallography

ChemPhysChem ◽

10.1002/cphc.202100098 ◽

2021 ◽

Author(s):

Emil Roduner ◽

Dominique M.S. Buyens ◽

Lynne A. Pilcher

Keyword(s):

Uv Spectroscopy ◽

Self Aggregation

Download Full-text

Fast and Resilient Manipulation Planning for Object Retrieval in Cluttered and Confined Environments

IEEE Transactions on Robotics ◽

10.1109/tro.2020.3047472 ◽

2021 ◽

pp. 1-14

Author(s):

Changjoo Nam ◽

Sang Hun Cheong ◽

Jinhwi Lee ◽

Dong Hwan Kim ◽

ChangHwan Kim

Keyword(s):

Object Retrieval ◽

Manipulation Planning

Download Full-text

Post-Processing Techniques for the Improvement of Liposome Stability

Pharmaceutics ◽

10.3390/pharmaceutics13071023 ◽

2021 ◽

Vol 13 (7) ◽

pp. 1023

Author(s):

Ji Young Yu ◽

Piyanan Chuesiang ◽

Gye Hwa Shin ◽

Hyun Jin Park

Keyword(s):

Freeze Drying ◽

Protective Agent ◽

Post Processing ◽

Additional Process ◽

Spray Freeze Drying ◽

The Stability ◽

Processing Techniques ◽

The Impact ◽

Self Aggregation ◽

Liposome Stability

Liposomes have been utilized as a drug delivery system to increase the bioavailability of drugs and to control the rate of drug release at the target site of action. However, the occurrence of self-aggregation, coalescence, flocculation and the precipitation of aqueous liposomes during formulation or storage can cause degradation of the vesicle structure, leading to the decomposition of liposomes. To increase the stability of liposomes, post-processing techniques have been applied as an additional process to liposomes after formulation to remove water and generate dry liposome particles with a higher stability and greater accessibility for drug administration in comparison with aqueous liposomes. This review covers the effect of these techniques including freeze drying, spray drying and spray freeze drying on the stability, physicochemical properties and drug encapsulation efficiency of dry liposomes. The parameters affecting the properties of liposomes during the drying process are also highlighted in this review. In addition, the impact of using a protective agent to overcome such limitations of each process is thoroughly discussed through various studies.

Download Full-text

Partial 3D Object Retrieval using Local Binary QUICCI Descriptors and Dissimilarity Tree Indexing

Computers & Graphics ◽

10.1016/j.cag.2021.07.018 ◽

2021 ◽

Author(s):

Bart Iver van Blokland ◽

Theoharis Theoharis

Keyword(s):

3D Object Retrieval ◽

Object Retrieval ◽

3D Object

Download Full-text

Self-aggregation behaviour of novel thiosemicarbazone drug candidates with potential antiviral activity

New Journal of Chemistry ◽

10.1039/c0nj00061b ◽

2010 ◽

Vol 34 (9) ◽

pp. 2047 ◽

Cited By ~ 23

Author(s):

Romina J. Glisoni ◽

Diego A. Chiappetta ◽

Liliana M. Finkielsztein ◽

Albertina G. Moglioni ◽

Alejandro Sosnik

Keyword(s):

Antiviral Activity ◽

Drug Candidates ◽

Aggregation Behaviour ◽

Self Aggregation

Download Full-text

Liquid–Liquid Phase Separation Enhances TDP-43 LCD Aggregation but Delays Seeded Aggregation

Biomolecules ◽

10.3390/biom11040548 ◽

2021 ◽

Vol 11 (4) ◽

pp. 548

Author(s):

Donya Pakravan ◽

Emiel Michiels ◽

Anna Bratek-Skicki ◽

Mathias De Decker ◽

Joris Van Lindt ◽

...

Keyword(s):

Phase Separation ◽

Liquid Phase ◽

Hydrophobic Interactions ◽

Low Complexity ◽

Liquid Phase Separation ◽

End Stage ◽

Positive Effect ◽

Self Aggregation ◽

Lateral Sclerosis ◽

Liquid Liquid Phase Separation

Aggregates of TAR DNA-binding protein (TDP-43) are a hallmark of several neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS). Although TDP-43 aggregates are an undisputed pathological species at the end stage of these diseases, the molecular changes underlying the initiation of aggregation are not fully understood. The aim of this study was to investigate how phase separation affects self-aggregation and aggregation seeded by pre-formed aggregates of either the low-complexity domain (LCD) or its short aggregation-promoting regions (APRs). By systematically varying the physicochemical conditions, we observed that liquid–liquid phase separation (LLPS) promotes spontaneous aggregation. However, we noticed less efficient seeded aggregation in phase separating conditions. By analyzing a broad range of conditions using the Hofmeister series of buffers, we confirmed that stabilizing hydrophobic interactions prevail over destabilizing electrostatic forces. RNA affected the cooperativity between LLPS and aggregation in a “reentrant” fashion, having the strongest positive effect at intermediate concentrations. Altogether, we conclude that conditions which favor LLPS enhance the subsequent aggregation of the TDP-43 LCD with complex dependence, but also negatively affect seeding kinetics.

Download Full-text