Molecular Architecture Influences the Thermally Induced Aggregation Behavior of Elastin-like Polypeptides

2011 ◽  
Vol 12 (11) ◽  
pp. 4022-4029 ◽  
Author(s):  
Ali Ghoorchian ◽  
Nolan B. Holland
Keyword(s):  
Aggregation Behavior ◽  
Molecular Architecture ◽  
Thermally Induced ◽  
Induced Aggregation

scholarly journals Thermoresponsive Polymers as Macromolecular Coordination Ligands: Complexation-Dependence of Thermally Induced Aggregation in Aqueous Solution

2021 ◽  
Author(s):  
Maximilian Felix Toni Meier ◽  
Franck Thetiot ◽  
Narsimhulu Pittala ◽  
Ingo Lieberwirth ◽  
Cleiton Kunzler ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Thermoresponsive Polymers ◽  
Thermally Induced ◽  
Coordination Sites ◽  
Induced Aggregation

We have designed novel macromolecular coordination ligands (MCLs) by conjugation of thermoresponsive polymers based on poly(N-isopropylacrylamide) (M ̅_n around 3 to 25 kg∙mol-1) with 1,2,4-triazole coordination sites. These triazole units...

scholarly journals Thermally induced aggregation of rigid spheres on a liquid surface

2016 ◽  
Vol 380 (1-2) ◽  
pp. 227-231
Author(s):  
Eric Forgoston ◽  
Leo Hentschker ◽  
Siobhan Soltau ◽  
Patrick Truitt ◽  
Ashwin Vaidya
Keyword(s):  
Liquid Surface ◽  
Rigid Spheres ◽  
Thermally Induced ◽  
Induced Aggregation

Chaperone-Like Activity of Human Haptoglobin: Similarity with α-Crystallin

1999 ◽  
Vol 64 (4) ◽  
pp. 717-725 ◽  
Author(s):  
Zdeněk Pavlíček ◽  
Rüdiger Ettrich
Keyword(s):  
Oxidative Stress ◽  
Thermally Induced ◽  
Genetic Types ◽  
Induced Aggregation ◽  
Sequence Similarities

Human haptoglobin (Hp) has been shown to have chaperone-like activity in preventing thermally induced aggregation of catalase and γ-crystallin. No differences in the chaperone- like behaviour of genetic types Hp 1-1 and a mixture of types Hp 2-1 and Hp 2-2 (i.e. Hp II) were found. Haptoglobin not only suppresses heat-induced aggregation of proteins but also prevents γ-crystallin from aggregation by oxidative stress. In addition, haptoglobin also provides protection against glycation-induced inactivation of catalase by glyceraldehyde. Chaperone-like activity of haptoglobin decreases in the course of its glycation. Refolding studies have shown that Hp exhibits its chaperone-like activity predominantly on the unfolding and not on the refolding pathway. Although Hp and α-crystallin have no sequence similarities, it seems that their chaperone-like activities are of the same type.

scholarly journals Buffer’s ionic strength on the chaperone-like activity (CLA) of silkworm small heat shock protein: sHSP19.9 and sHSP20.8

2016 ◽  
Vol 12 (2) ◽  
pp. 241-249
Author(s):  
M Tofazzal Hossain ◽  
Yoichi Aso
Keyword(s):  
Ionic Strength ◽  
Heat Shock ◽  
Small Heat Shock Protein ◽  
High Ionic Strength ◽  
Thermally Induced ◽  
Native Proteins ◽  
Chemically Induced ◽  
Irreversible Aggregation ◽  
Shock Proteins ◽  
Induced Aggregation

Small heat-shock proteins (sHSPs), an abundant and ubiquitous family of molecular chaperones, can effectively prevent irreversible aggregation of non-native proteins by forming soluble complex. The CLA of sHSPs is usually determined by the capacity to suppress thermally or chemically induced protein aggregation. Various factors can effectively influence the CLA, and among them the ionic strength of the preparation and working buffer is an important factor. The study deals with the effect of ionic strength of buffer on the CLA of two silkworm sHSPs: namely sHSP19.9 and sHSP20.8 against the thermally-induced aggregation of BLC, a non-native protein. The study clearly revealed that sHSP19.9 required high ionic strength (more NaCl concentration) in reaction buffer to prevent irreversible aggregation of BLC. On the other hand, such high ionic strength condition is not necessary for sHSP20.8 but it influences the activity in some context.J. Bangladesh Agril. Univ. 12(2): 241-249, December 2014

scholarly journals Thermally induced aggregation and its suppression of silkworm small heat shock protein sHSP19.9

2017 ◽  
Vol 46 (1) ◽  
pp. 57-64
Author(s):  
MT Hossain ◽  
Y Aso
Keyword(s):  
Ionic Strength ◽  
Heat Shock ◽  
Molecular Chaperone ◽  
Reaction Medium ◽  
Small Heat Shock Protein ◽  
Time Dependent ◽  
Thermally Induced ◽  
Shock Proteins ◽  
Low Ionic Strength ◽  
Induced Aggregation

About ten genes responsible for small heat-shock proteins (sHSP) have been isolated from silkworm. sHSP19.9 is one of the important member among them. Heat-induced stability of the sHSP was investigated at 60ºC with 20 mM HEPES buffer pH 7.7 containing 10 mM NaCl (low-ionic strength). Along with it probable suppression of the aggregation was also examined. At the mentioned reaction medium, sHSP19.9 was observed to be aggregated on the concentration- and time-dependent manners. It was successfully suppressed with dithiothreitol (DTT), higher-ionic strengths, Cysteine residues modifications and molecular chaperone: sHSP20.8.Bang. J. Anim. Sci. 2017. 46 (1): 57-64

Sign in / Sign up

Export Citation Format

Share Document