scholarly journals Role of a Novel Excipient Poly(ethylene glycol)-b-poly(l-histidine) in Retention of Physical Stability of Insulin at Aqueous/Organic Interface

2007 ◽  
Vol 4 (4) ◽  
pp. 561-570 ◽  
Author(s):  
Ajay Taluja ◽  
You Han Bae
Keyword(s):  
Ethylene Glycol ◽  
Physical Stability ◽  
Poly Ethylene Glycol ◽  
Poly Ethylene

scholarly journals The role of poly(ethylene glycol) brush architecture in complement activation on targeted microbubble surfaces

Biomaterials ◽  
2011 ◽  
Vol 32 (27) ◽  
pp. 6579-6587 ◽  
Author(s):  
Cherry C. Chen ◽  
Mark A. Borden
Keyword(s):  
Ethylene Glycol ◽  
Complement Activation ◽  
Poly Ethylene Glycol ◽  
Poly Ethylene

The role of hydrogen bonding in alginate/poly(acrylamide-co-dimethylacrylamide) and alginate/poly(ethylene glycol) methyl ether methacrylate-based tough hybrid hydrogels

RSC Advances ◽  
2015 ◽  
Vol 5 (71) ◽  
pp. 57678-57685 ◽  
Author(s):  
Zhi Wei Low ◽  
Pei Lin Chee ◽  
Dan Kai ◽  
Xian Jun Loh
Keyword(s):  
Hydrogen Bonding ◽  
Elastic Modulus ◽  
Ethylene Glycol ◽  
Methyl Ether ◽  
Poly Ethylene Glycol ◽  
Hybrid Hydrogels ◽  
Poly Ethylene ◽  
Glycol Methyl Ether ◽  
Poly Acrylamide

Hybrid hydrogels, with an elastic modulus and compressive toughness of 350 kPa and 70 J m−3, was synthesized and reported here.

Investigation of the role of hydrophilic chain length in amphiphilic perfluoropolyether/poly(ethylene glycol) networks: towards high-performance antifouling coatings

Biofouling ◽  
2011 ◽  
Vol 27 (10) ◽  
pp. 1139-1150 ◽  
Author(s):  
Yapei Wang ◽  
Louis M. Pitet ◽  
John A. Finlay ◽  
Lenora H. Brewer ◽  
Gemma Cone ◽  
...  
Keyword(s):  
Ethylene Glycol ◽  
Chain Length ◽  
High Performance ◽  
Poly Ethylene Glycol ◽  
Antifouling Coatings ◽  
Poly Ethylene

scholarly journals Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues

1997 ◽  
Vol 325 (3) ◽  
pp. 685-691 ◽  
Author(s):  
Desong CHEN ◽  
R. Manjunatha KINI ◽  
Raymond YUEN ◽  
Hoon Eng KHOO
Keyword(s):  
Cell Membrane ◽  
Ethylene Glycol ◽  
Haemolytic Activity ◽  
Side Chains ◽  
Poly Ethylene Glycol ◽  
Arginine Residues ◽  
Poly Ethylene ◽  
Cationic Residues ◽  
Positively Charged

Stonustoxin (SNTX) is a two-subunit protein toxin purified from the venom of the stonefish (Synanceja horrida), which induces potent haemolytic activity. We examined the pore-forming property of this non-enzymic protein by an osmotic protection assay. SNTX-induced haemolysis was completely prevented by osmotic protectants of adequate size [poly(ethylene) glycol 3000; molecular diameter approx. 3.2 nm]. Uncharged molecules of smaller size, such as raffinose and poly(ethylene) glycol 1000–2000, failed to protect against cell lysis. These findings indicate that SNTX induces the formation of hydrophilic pores in the cell membrane, which results in the lysis of erythrocytes. Since cationic residues contribute significantly to the cytolytic activity of several other pore-forming toxins, we examined the role of positively charged lysine and arginine residues in the haemolytic activity of SNTX. SNTX lost its haemolytic activity when the positively charged side chains of lysine residues were neutralized or converted into negatively charged side chains upon carbamylation or succinylation respectively. The haemolytic activity of SNTX was also inhibited by the modification of positively charged arginine residues using 2,3-butanedione. The loss of haemolysis showed strong correlation with the number of Lys or Arg residues modified. CD analyses, however, showed that the conformation of SNTX was not significantly affected by these chemical modifications. Further, the haemolytic activity of SNTX was competitively inhibited by various negatively charged lipids, such as phosphatidylserine, cardiolipin and monosialogangliosides. These results indicate that SNTX induces potent haemolytic activity through the formation of pores in the cell membrane, and that cationic residues play a crucial role in its cytolytic mechanism.

Sign in / Sign up

Export Citation Format

Share Document