The role of sucrose concentration in self-assembly kinetics of high methoxyl pectin

2018 ◽  
Vol 112 ◽  
pp. 1183-1190 ◽  
Author(s):  
Daniela Giacomazza ◽  
Donatella Bulone ◽  
Pier Luigi San Biagio ◽  
Rosamaria Marino ◽  
Romano Lapasin
Langmuir ◽  
2012 ◽  
Vol 28 (21) ◽  
pp. 7962-7966 ◽  
Author(s):  
Jianhao Wang ◽  
Pengju Jiang ◽  
Zuoyan Han ◽  
Lin Qiu ◽  
Cheli Wang ◽  
...  

2017 ◽  
Vol 50 (4) ◽  
pp. 1657-1665 ◽  
Author(s):  
Cuiyun Zhang ◽  
You Fan ◽  
Yunyi Zhang ◽  
Cong Yu ◽  
Hongfei Li ◽  
...  

2021 ◽  
Author(s):  
Arabinda Behera ◽  
Oshin Sharma ◽  
Debjani Paul ◽  
Anirban Sain

Molecular self-assembly plays vital role in various biological functions. However, when aberrant molecules self-assemble to form large aggregates, it can give rise to various diseases. For example, the sickle cell disease and Alzheimer’s disease are caused by self-assembled hemoglobin fibers and amyloid plaques, respectively. Here we study the assembly kinetics of such fibers using kinetic Monte-Carlo simulation. We focus on the initial lag time of these highly stochastic processes, during which self-assembly is very slow. The lag time distributions turn out to be similar for two very different regimes of polymerization, namely, a) when polymerization is slow and depolymerization is fast, and b) the opposite case, when polymerization is fast and depolymerization is slow. Using temperature dependent on- and off-rates for hemoglobin fiber growth, reported in recent in-vitro experiments, we show that the mean lag time can exhibit non-monotonic behaviour with respect to change of temperature.


2015 ◽  
Vol 7 (46) ◽  
pp. 25843-25850 ◽  
Author(s):  
Woon Ik Park ◽  
Young Joong Choi ◽  
Je Moon Yun ◽  
Suck Won Hong ◽  
Yeon Sik Jung ◽  
...  

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 596
Author(s):  
Nguyen Truong Co ◽  
Mai Suan Li

The self-assembly of amyloidogenic peptides and proteins into fibrillar structures has been intensively studied for several decades, because it seems to be associated with a number of neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. Therefore, understanding the molecular mechanisms of this phenomenon is important for identifying an effective therapy for the corresponding diseases. Protein aggregation in living organisms very often takes place on surfaces like membranes and the impact of a surface on this process depends not only on the surface chemistry but also on its topology. Our goal was to develop a simple lattice model for studying the role of surface roughness in the aggregation kinetics of polypeptide chains and the morphology of aggregates. We showed that, consistent with the experiment, an increase in roughness slows down the fibril formation, and this process becomes inhibited at a very highly level of roughness. We predicted a subtle catalytic effect that a slightly rough surface promotes the self-assembly of polypeptide chains but does not delay it. This effect occurs when the interaction between the surface and polypeptide chains is moderate and can be explained by taking into account the competition between energy and entropy factors.


2015 ◽  
Vol 17 (17) ◽  
pp. 11182-11192 ◽  
Author(s):  
David Abbasi-Pérez ◽  
J. Manuel Recio ◽  
Lev Kantorovich

para-Terphenyl-meta-dicarbonitrile molecules diffuse by pivoting on the Ag(111) surface, and by means of the assisted isomerization mechanism self-assemble to form ribbons, linkers, clusters and brickwall islands.


2016 ◽  
Vol 13 (114) ◽  
pp. 20150762 ◽  
Author(s):  
A. A. Lee ◽  
M. J. Senior ◽  
M. I. Wallace ◽  
T. E. Woolley ◽  
I. M. Griffiths

Pore-forming toxins are ubiquitous cytotoxins that are exploited by both bacteria and the immune response of eukaryotes. These toxins kill cells by assembling large multimeric pores on the cell membrane. However, a quantitative understanding of the mechanism and kinetics of this self-assembly process is lacking. We propose an analytically solvable kinetic model for stepwise, reversible oligomerization. In biologically relevant limits, we obtain simple algebraic expressions for the rate of pore formation, as well as for the concentration of pores as a function of time. Quantitative agreement is obtained between our model and time-resolved kinetic experiments of Bacillus thuringiensis Cry1Ac (tetrameric pore), aerolysin, Staphylococcus aureus α -haemolysin (heptameric pores) and Escherichia coli cytolysin A (dodecameric pore). Furthermore, our model explains how rapid self-assembly can take place with low concentrations of oligomeric intermediates, as observed in recent single-molecule fluorescence experiments of α-haemolysin self-assembly. We propose that suppressing the concentration of oligomeric intermediates may be the key to reliable, error-free, self-assembly of pores.


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