scholarly journals ESI-IMS–MS: A method for rapid analysis of protein aggregation and its inhibition by small molecules

Methods ◽  
2016 ◽  
Vol 95 ◽  
pp. 62-69 ◽  
Author(s):  
Lydia M. Young ◽  
Janet C. Saunders ◽  
Rachel A. Mahood ◽  
Charlotte H. Revill ◽  
Richard J. Foster ◽  
...  
2012 ◽  
Vol 8 (4S_Part_17) ◽  
pp. P637-P637
Author(s):  
Judy Cam ◽  
Joel Cummings ◽  
Thomas Lake ◽  
Kelsey Hanson ◽  
Luke Esposito ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (6) ◽  
pp. 1380 ◽  
Author(s):  
Hoon Suk Rho ◽  
Henk-Willem Veltkamp ◽  
Alexander Thomas Hanke ◽  
Marcel Ottens ◽  
Christian Breukers ◽  
...  

A microfluidic protein aggregation device (microPAD) that allows the user to perform a series of protein incubations with various concentrations of two reagents is demonstrated. The microfluidic device consists of 64 incubation chambers to perform individual incubations of the protein at 64 specific conditions. Parallel processes of metering reagents, stepwise concentration gradient generation, and mixing are achieved simultaneously by pneumatic valves. Fibrillation of bovine insulin was selected to test the device. The effect of insulin and sodium chloride (NaCl) concentration on the formation of fibrillar structures was studied by observing the growth rate of partially folded protein, using the fluorescent marker Thioflavin-T. Moreover, dual gradients of different NaCl and hydrochloric acid (HCl) concentrations were formed, to investigate their interactive roles in the formation of insulin fibrils and spherulites. The chip-system provides a bird’s eye view on protein aggregation, including an overview of the factors that affect the process and their interactions. This microfluidic platform is potentially useful for rapid analysis of the fibrillation of proteins associated with many misfolding-based diseases, such as quantitative and qualitative studies on amyloid growth.


2017 ◽  
Vol 5 (3) ◽  
pp. 485-493 ◽  
Author(s):  
Miaoyi Wang ◽  
Aleksandr Kakinen ◽  
Emily H. Pilkington ◽  
Thomas P. Davis ◽  
Pu Chun Ke

Recent studies have shown promise on the use of small molecules and nanoparticles (NPs) for the inhibition of protein aggregation, a hallmark of neurodegenerative diseases and type 2 diabetes (T2D).


2011 ◽  
Vol 7 ◽  
pp. S481-S481 ◽  
Author(s):  
Qubai Hu ◽  
Judy Cam ◽  
Thomas Lake ◽  
Joel Cummings ◽  
Luke Esposito ◽  
...  

Biologia ◽  
2013 ◽  
Vol 68 (5) ◽  
Author(s):  
Arezou Ghahghaei ◽  
Monavar Neyestani

AbstractAmyloids are insoluble fibers which arise from inappropriately folded versions of proteins and have been associated with the pathology of many neurodegenerative diseases. α-Casein is one of the major components of the casein family which is known to show chaperone-like activity. Glycerol is a polyol compound which acts as a chemical chaperone to increase protein stability and inhibit protein aggregation. In this study, the effect of arginine and glycine on the chaperone ability of α-casein and glycerol against order aggregation of κ-casein was investigated and compared. We found that these additives reduced the chaperone ability of α-casein against the amyloid formation of κ-casein, especially in the presence of arginine. Importantly, our results show that the chaperone action of glycerol is enhanced in the presence of both arginine and glycine. Accordingly, our results suggest that these small molecules associated with glycerol, especially glycine, should be considered as a mechanism for the treatment of amyloid disease.


Author(s):  
James R. Gaylor ◽  
Fredda Schafer ◽  
Robert E. Nordquist

Several theories on the origin of the melanosome exist. These include the Golgi origin theory, in which a tyrosinase-rich protein is "packaged" by the Golgi apparatus, thus forming the early form of the melanosome. A second theory postulates a mitochondrial origin of melanosomes. Its author contends that the melanosome is a modified mitochondria which acquires melanin during its development. A third theory states that a pre-melanosome is formed in the smooth or rough endoplasmic reticulum. Protein aggregation is suggested by one author as a possible source of the melanosome. This fourth theory postulates that the melanosome originates when the protein products of several genetic loci aggregate in the cytoplasm of the melanocyte. It is this protein matrix on which the melanin is deposited. It was with these theories in mind that this project was undertaken.


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