2008
DOI: 10.1016/j.bbagen.2007.08.017
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Multi-block poloxamer surfactants suppress aggregation of denatured proteins

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Cited by 42 publications
(32 citation statements)
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“…Alexandridis, Holzwarth, and Hatton (1994) found that a negative entropy contribution caused by the removal of highly oriented clathrate cages of water molecules surrounding the non-polar block of Pluronics is the main driving force of micellarization. PF-68 was shown to facilitate re-folding and suppress the aggregation of thermally unfolded proteins (Mustafi, Smith, Makinen, & Lee, 2008). The model for surfactant-protein interaction (Lee et al, 2011) showed that in the case of a low-surfactant concentration below the CMC, the molecules of the surfactant are localized on the surface of the liquid phase and only a limited number of surfactant molecules are bound to the surface of the protein.…”
Section: Discussionmentioning
confidence: 99%
“…Alexandridis, Holzwarth, and Hatton (1994) found that a negative entropy contribution caused by the removal of highly oriented clathrate cages of water molecules surrounding the non-polar block of Pluronics is the main driving force of micellarization. PF-68 was shown to facilitate re-folding and suppress the aggregation of thermally unfolded proteins (Mustafi, Smith, Makinen, & Lee, 2008). The model for surfactant-protein interaction (Lee et al, 2011) showed that in the case of a low-surfactant concentration below the CMC, the molecules of the surfactant are localized on the surface of the liquid phase and only a limited number of surfactant molecules are bound to the surface of the protein.…”
Section: Discussionmentioning
confidence: 99%
“…This non-ionic surfactant, comprised of hydrophobic and hydrophilic segments will surround and protect the protein by limiting its adsorption onto the hydrophobic surface of the PLGA polymer (Morille et al, 2013;Mustafi et al, 2008). It was co-precipitated with CST at the 415 ratio of 1:20 of protein:additive polymer, and allowed a complete release of CST.…”
Section: Discussionmentioning
confidence: 99%
“…Besides the effects on MMPs, surfactants can also suppress protein aggregation and aid refolding of denatured proteins to prevent persistent inflammation, which may lead to a non‐healing wound. Mustafi et al found that amphiphilic, surfactant, multi‐block copolymers, such as Poloxamer 108 (P108), Poloxamer 188 (P188), and Tetronic 1107 (T1107) are efficient as additives to suppress aggregation of and to facilitate refolding of heat‐denatured hen egg white lysozyme (HEWL) and bovine serum albumin (BSA) in solution. Additionally, Lee et al demonstrated that poloxamers are more efficient than PEG in preventing aggregation of heat denaturized lysozyme.…”
Section: Mode Of Action Of Surfactants In Wound Healingmentioning
confidence: 99%