Effect of protein–protein interactions on protein aggregation kinetics

2003 ◽  
Vol 119 (20) ◽  
pp. 10972-10976 ◽  
Author(s):  
Jing Zhang ◽  
Xiang Y. Liu
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Aggregation Kinetics ◽  
Protein Protein Interactions

Evolutionary selection for protein aggregation

2012 ◽  
Vol 40 (5) ◽  
pp. 1032-1037 ◽  
Author(s):  
Natalia Sanchez de Groot ◽  
Marc Torrent ◽  
Anna Villar-Piqué ◽  
Benjamin Lang ◽  
Salvador Ventura ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Current Knowledge ◽  
Protein Aggregates ◽  
Cellular Systems ◽  
Aggregation Process ◽  
Loss Of Function ◽  
Protein Protein Interactions ◽  
Wide Range ◽  
Range Of Functions

Protein aggregation is being found to be associated with an increasing number of human diseases. Aggregation can lead to a loss of function (lack of active protein) or to a toxic gain of function (cytotoxicity associated with protein aggregates). Although potentially harmful, protein sequences predisposed to aggregation seem to be ubiquitous in all kingdoms of life, which suggests an evolutionary advantage to having such segments in polypeptide sequences. In fact, aggregation-prone segments are essential for protein folding and for mediating certain protein–protein interactions. Moreover, cells use protein aggregates for a wide range of functions. Against this background, life has adapted to tolerate the presence of potentially dangerous aggregation-prone sequences by constraining and counteracting the aggregation process. In the present review, we summarize the current knowledge of the advantages associated with aggregation-prone stretches in proteomes and the strategies that cellular systems have developed to control the aggregation process.

P3-295: Breaking protein-protein interactions: A combined chemical and computational approach to develop a new class of protein aggregation inhibitors

2009 ◽  
Vol 5 (4S_Part_14) ◽  
pp. P429-P430
Author(s):  
Isabella Graef ◽  
Mamoun M. Alhamadsheh ◽  
Alexandra Esteras-Chopo ◽  
Kim Branson ◽  
Mohua Bose ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Computational Approach ◽  
Protein Protein Interactions ◽  
New Class ◽  
Aggregation Inhibitors

scholarly journals Polysorbate 80 Controls Morphology, Structure and Stability of Human Insulin Amyloid-Like Spherulites

2021 ◽  
Author(s):  
Xin Zhou ◽  
Dirk Fennema Galparsoro ◽  
Anders Oestergaard Madsen ◽  
Valeria Vetri ◽  
Marco van de Weert ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Human Insulin ◽  
Protein Interactions ◽  
Physicochemical Characteristics ◽  
Beta Sheets ◽  
Aggregation Kinetics ◽  
Polysorbate 80 ◽  
Protein Protein Interactions ◽  
Dynamics Simulations

Amyloid protein aggregates are not only associated with neurodegenerative diseases and may also occur as unwanted by-products in protein-based therapeutics. Surfactants are often employed to stabilize protein formulations and reduce the risk of aggregation. However, surfactants alter protein-protein interactions and may thus modulate the physicochemical characteristics of any aggregates formed. Human insulin aggregation was induced at low pH in the presence of varying concentrations of the surfactant polysorbate 80. Various spectroscopic and imaging methods were used to study the aggregation kinetics, as well as structure and morphology of the formed aggregates. Molecular dynamics simulations were employed to investigate the initial interaction between the surfactant and insulin. Addition of polysorbate 80 slowed down, but did not prevent, aggregation of insulin. Amyloid spherulites formed under all conditions, with a higher content of intermolecular beta-sheets in the presence of the surfactant above its critical micelle concentration. In addition, a denser packing was observed, leading to a more stable aggregate. Molecular dynamics simulations suggested a tendency for insulin to form dimers in the presence of the surfactant, indicating a change in protein-protein interactions. It is thus shown that surfactants not only alter aggregation kinetics, but also affect physicochemical properties of any aggregates formed.

Protein-protein interactions of the p53 family with the Bcl-2 family in hepatocellular carcinoma

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
LC König ◽  
M Meinhard ◽  
C Sandig ◽  
MH Bender ◽  
A Lovas ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
P53 Family
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