Stabilization of Enzyme by Using Hydrophobic Ligands.

Artificial Chaperone-Assisted Refolding of Bovine Carbonic Anhydrase Using Molecular Assemblies of Stimuli-Responsive Polymers

“…It has also been demonstrated that the reactivation yield of CAB is enhanced by the addition of a molecular chaperone (such as GroELp), liposomes, and hydrophobic ligands (such as PEG and Triton X-series). − ,, It has also been reported that the local hydrophobicity of the chaperones and the other chaperone-like materials could play an important role in the refolding of denatured proteins. , As shown in Figure , PPO n −Ph−PEG, which has been used in this study, has a hydrophobic headgroup (PPO n −Ph group) and a hydrophilic tail (PEG) along the molecules. The effect of the type of headgroup bound to the PEG molecule has already been investigated, and the hydrophobicity of the headgroup was shown to be an important factor in interaction with the CAB in the intermediate state. Similarly in this case, the local hydrophobicity of PPO−Ph−PEG at various temperatures was considered to be an effective factor governing the refolding process of CAB.…”

“…It has also been demonstrated that the reactivation yield of CAB is enhanced by the addition of a molecular chaperone (such as GroELp), liposomes, and hydrophobic ligands (such as PEG and Triton X-series). [11][12][13]15,16 It has also been reported that the local hydrophobicity of the chaperones and the other chaperone-like materials could play an important role in the refolding of denatured proteins. 12,14 As shown in Figure 1, PPO n -Ph-PEG, which has been used in this study, has a hydrophobic headgroup (PPO n -Ph group) and a hydrophilic tail (PEG) along the molecules.…”

“…12,14 As shown in Figure 1, PPO n -Ph-PEG, which has been used in this study, has a hydrophobic headgroup (PPO n -Ph group) and a hydrophilic tail (PEG) along the molecules. The effect of the type of headgroup bound to the PEG molecule has already been investigated, 16 and the hydrophobicity of the headgroup was shown to be an important factor in interaction with the CAB in the intermediate state. Similarly in this case, the local hydrophobicity of PPO-Ph-PEG at various temperatures was considered to be an effective factor governing the refolding process of CAB.…”

“…10,11 The evaluated local hydrophobicity of a protein was found to play an important role not only in the protein denaturation or aggregate-formation processes 10,11 but also in interaction with liposomes, [12][13][14] heat shock proteins, 15 and hydrophobic ligands. 16 A biomimetic material, which can improve the reactivation yield of denatured protein and is known as an "artificial chaperone", 17 can be designed and developed based on the quantitative surface properties of the target protein and chaperones (i.e., liposomes and GroEL). In the early 1990s, Cleland and co-workers first investigated the chaperone-like function of the amphiphilic polymer (poly(ethylene glycol)).…”

“…The protein in this state is known to have a secondary structure like the native state but does not have a closely packed tertiary structure. , Recently, a systematic approach on the protein folding process has been reported in a series of works related to the evaluated values of proteins in various conformations . The variation of the surface properties of proteins during their denaturation and refolding processes can be quantitatively characterized using the aqueous two-phase partitioning method. , The evaluated local hydrophobicity of a protein was found to play an important role not only in the protein denaturation or aggregate-formation processes 10,11 but also in interaction with liposomes, − heat shock proteins, and hydrophobic ligands . A biomimetic material, which can improve the reactivation yield of denatured protein and is known as an “artificial chaperone”, can be designed and developed based on the quantitative surface properties of the target protein and chaperones (i.e., liposomes and GroEL).…”