basic polypeptide
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2020 ◽  
Vol 30 (3) ◽  
pp. 126890
Author(s):  
Peter V. Dubovskii ◽  
Anastasia A. Ignatova ◽  
Alexey V. Feofanov ◽  
Yuri N. Utkin ◽  
Roman G. Efremov

LWT ◽  
2019 ◽  
Vol 114 ◽  
pp. 108328 ◽  
Author(s):  
Hou-Qi Ning ◽  
Zhao-Sheng Wang ◽  
Ying-Qiu Li ◽  
Wen-Li Tian ◽  
Gui-Jin Sun ◽  
...  

LWT ◽  
2017 ◽  
Vol 83 ◽  
pp. 267-274 ◽  
Author(s):  
Jin Hou ◽  
Ying-Qiu Li ◽  
Zhao-Sheng Wang ◽  
Gui-Jin Sun ◽  
Hai-Zhen Mo
Keyword(s):  

2016 ◽  
Vol 25 (5) ◽  
pp. 1477-1483 ◽  
Author(s):  
Jie Yang ◽  
Gui-Jin Sun ◽  
Ying-Qiu Li ◽  
Kai-Yu Cui ◽  
Hai Zhen Mo

2016 ◽  
Vol 25 (3) ◽  
pp. 803-809 ◽  
Author(s):  
Ying-Qiu Li ◽  
Man Hao ◽  
Jie Yang ◽  
Hai-Zhen Mo

2014 ◽  
Vol 10 ◽  
pp. 707-713 ◽  
Author(s):  
Li Zhao ◽  
Yuki Nakae ◽  
Hongmei Qin ◽  
Tadamasa Ito ◽  
Takahide Kimura ◽  
...  

A gene vector consisting of nanodiamond, polyglycerol, and basic polypeptide (ND-PG-BPP) has been designed, synthesized, and characterized. The ND-PG-BPP was synthesized by PG functionalization of ND through ring-opening polymerization of glycidol on the ND surface, multistep organic transformations (–OH → –OTs (tosylate) → –N3) in the PG layer, and click conjugation of the basic polypeptides (Arg8, Lys8 or His8) terminated with propargyl glycine. The ND-PG-BPP exhibited good dispersibility in water (>1.0 mg/mL) and positive zeta potential ranging from +14.2 mV to +44.1 mV at neutral pH in Milli-Q water. It was confirmed by gel retardation assay that ND-PG-Arg8 and ND-PG-Lys8 with higher zeta potential hybridized with plasmid DNA (pDNA) through electrostatic attraction, making them promising as nonviral vectors for gene delivery.


2013 ◽  
Vol 69 (10) ◽  
pp. 1958-1964 ◽  
Author(s):  
Monika A. Coronado ◽  
Azat Gabdulkhakov ◽  
Dessislava Georgieva ◽  
Banumathi Sankaran ◽  
Mario T. Murakami ◽  
...  

The crystal structure of the myotoxic, cell-penetrating, basic polypeptide crotamine isolated from the venom ofCrotalus durissus terrificushas been determined by single-wavelength anomalous dispersion techniques and refined at 1.7 Å resolution. The structure reveals distinct cationic and hydrophobic surface regions that are located on opposite sides of the molecule. This surface-charge distribution indicates its possible mode of interaction with negatively charged phospholipids and other molecular targets to account for its diverse pharmacological activities. Although the sequence identity between crotamine and human β-defensins is low, the three-dimensional structures of these functionally related peptides are similar. Since crotamine is a leading member of a large family of myotoxic peptides, its structure will provide a basis for the design of novel cell-penetrating molecules.


Toxicon ◽  
2005 ◽  
Vol 46 (4) ◽  
pp. 363-370 ◽  
Author(s):  
N. Oguiura ◽  
M. Boni-Mitake ◽  
G. Rádis-Baptista

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