linear polyacrylamide
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ASJ. ◽  
2021 ◽  
Vol 1 (56) ◽  
pp. 04-11
Author(s):  
V. Lakhtin ◽  
M. Lakhtin ◽  
A. Melikhova ◽  
I. Davydkin ◽  
V. Davydkin ◽  
...  

The overview focuses on our own data on the use of water-soluble glycoconjugates (www.lectinity.com) based on a linear polyacrylamide chain in relation to recombinant therapeutic human protein hormones and probiotic recognition proteins such as enzymes and lectins. The results obtained characterize the basic principles of multilevel relationships between proteins and glycoconjugates, including the assembly of complexes and nanoparticles on the solid phase. Prospects for the application of these principles and cases of interaction of proteins and glycoconjugates, including taking into account the participation of enzymes, in the study of human proteins and viruses, are noted. The presented data can help in development of the protective network communication systems as well as new combined preparations against infections and pathogens. These data can serve the keys to be applied in medical biotechnology. 


Author(s):  
Frank Maixner ◽  
Christian Mitterer ◽  
Heidi Y. Jäger ◽  
Mohamed S. Sarhan ◽  
Guido Valverde ◽  
...  

2021 ◽  
Vol 22 (4) ◽  
pp. 1524
Author(s):  
Taro Shimamoto ◽  
Tatsuki Nakakubo ◽  
Tomoyasu Noji ◽  
Shuhei Koeda ◽  
Keisuke Kawakami ◽  
...  

The development of techniques capable of using membrane proteins in a surfactant-free aqueous buffer is an attractive research area, and it should be elucidated for various membrane protein studies. To this end, we examined a method using new solubilization surfactants that do not detach from membrane protein surfaces once bound. The designed solubilization surfactants, DKDKC12K-PAn (n = 5, 7, and 18), consist of two parts: one is the lipopeptide-based solubilization surfactant part, DKDKC12K, fand the other is the covalently connected linear polyacrylamide (PA) chain with different Mw values of 5, 7, or 18 kDa. Intermolecular interactions between the PA chains in DKDKC12K-PAn concentrated on the surfaces of membrane proteins via amphiphilic binding of the DKDKC12K part to the integral membrane domain was observed. Therefore, DKDKC12K-PAn (n = 5, 7, and 18) could maintain a bound state even after removal of the unbound by ultrafiltration or gel-filtration chromatography. We used photosystem I (PSI) from Thermosynecoccus vulcanus as a representative to assess the impacts of new surfactants on the solubilized membrane protein structure and functions. Based on the maintenance of unique photophysical properties of PSI, we evaluated the ability of DKDKC12K-PAn (n = 5, 7, and 18) as a new solubilization surfactant.


Talanta ◽  
2016 ◽  
Vol 150 ◽  
pp. 546-552 ◽  
Author(s):  
Miriam Beneito-Cambra ◽  
Philippe Anres ◽  
Jérôme Vial ◽  
Pierre Gareil ◽  
Nathalie Delaunay

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