Faculty Opinions recommendation of Rapid microtubule self-assembly kinetics.

Author(s):  
Linda Amos
2015 ◽  
Vol 21 (S3) ◽  
pp. 945-946
Author(s):  
Taylor J. Woehl ◽  
Tanya Prozorov

Langmuir ◽  
2012 ◽  
Vol 28 (21) ◽  
pp. 7962-7966 ◽  
Author(s):  
Jianhao Wang ◽  
Pengju Jiang ◽  
Zuoyan Han ◽  
Lin Qiu ◽  
Cheli Wang ◽  
...  

2018 ◽  
Vol 140 (7) ◽  
pp. 2619-2628 ◽  
Author(s):  
Jiangping Xu ◽  
Hang Zhou ◽  
Qing Yu ◽  
Ian Manners ◽  
Mitchell A. Winnik

2018 ◽  
Vol 112 ◽  
pp. 1183-1190 ◽  
Author(s):  
Daniela Giacomazza ◽  
Donatella Bulone ◽  
Pier Luigi San Biagio ◽  
Rosamaria Marino ◽  
Romano Lapasin

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

2013 ◽  
Vol 66 (5) ◽  
pp. 572 ◽  
Author(s):  
Richard J. Williams ◽  
James Gardiner ◽  
Anders B. Sorensen ◽  
Silvia Marchesan ◽  
Roger J. Mulder ◽  
...  

The early stages of the self-assembly of peptide hydrogels largely determine their final material properties. Here we discuss experimental methodologies for monitoring the self-assembly kinetics which underpin peptide hydrogel formation. The early stage assembly of an enzyme-catalysed Fmoc-trileucine based self-assembled hydrogel was examined using spectroscopic techniques (circular dichroism, CD, and solution NMR) as well as chromatographic (HPLC) and mechanical (rheology) techniques. Optimal conditions for enzyme-assisted hydrogel formation were identified and the kinetics examined. A lag time associated with the formation and accumulation of the self-assembling peptide monomer was observed and a minimum hydrogelator concentration required for gelation was identified. Subsequent formation of well defined nano- and microscale structures lead to self-supporting hydrogels at a range of substrate and enzyme concentrations. 1H NMR monitoring of the early self-assembly process revealed trends that were well in agreement with those identified using traditional methods (i.e. HPLC, CD, rheology) demonstrating 1H NMR spectroscopy can be used to non-invasively monitor the self-assembly of peptide hydrogels without damaging or perturbing the system.


2021 ◽  
Author(s):  
Alisha J. Lewis ◽  
Mathew M. Maye

In this paper, we describe the use of weakly interacting DNA linkages to assemble nanoparticles into defined clusters. Gold nanoparticles (AuNPs) were synthesized and functionalized with thiol modified single-stranded DNA (ssDNA) and hybridized with ssDNA linkers of a defined length (L). The self-assembly kinetics were altered by manipulating interparticle energetics through changes to linker length, rigidity, and sequence. The linker length regulated the hybridization energy between complementary AuNPs, were longer L increased adhesion, resulting in classical uncontrollable aggregation. In contrast, L of six complementary bases decreased adhesion and resulting in slower nucleation that promoted small cluster formation, the growth of which was studied at two assembly temperatures. Results indicated that a decrease in temperature to 15 oC increased cluster yield with L6 as compared to 25 oC. Finally, the clusters were separated from unassembled AuNPs by sucrose gradient ultracentrifugation (UC) and studied via UV-visible spectrophotometry (UV-vis), dynamic light scattering (DLS) and transmission electron microscopy (TEM).


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.


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