2006
DOI: 10.1002/jps.20715
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Effects of Cyclodextrins on Chemically and Thermally Induced Unfolding and Aggregation of Lysozyme and Basic Fibroblast Growth Factor

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Cited by 49 publications
(34 citation statements)
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“…As a result, research on this subject has attracted the attention of biologists, chemists, pharmacists, and therapists. [6][7][8][9][10][11][12] Protein stability and folding pathways are closely dependent on the various solvent ionic compositions, temperature, and adsorption on a hydrophobic surface. Excipients/additives, including cyclodextrins (CDs), can be added to the protein preparation commonly in order to inhibit protein denaturation.…”
Section: Introductionmentioning
confidence: 99%
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“…As a result, research on this subject has attracted the attention of biologists, chemists, pharmacists, and therapists. [6][7][8][9][10][11][12] Protein stability and folding pathways are closely dependent on the various solvent ionic compositions, temperature, and adsorption on a hydrophobic surface. Excipients/additives, including cyclodextrins (CDs), can be added to the protein preparation commonly in order to inhibit protein denaturation.…”
Section: Introductionmentioning
confidence: 99%
“…Protein stability is a particularly relevant issue in the pharmaceutical field and will continue to gain more importance as the number of therapeutic protein products increases. [5,6] Interactions between serum albumin and ligands can provide important information about ligand storage, transportation, evacuation, etc. As a result, research on this subject has attracted the attention of biologists, chemists, pharmacists, and therapists.…”
Section: Introductionmentioning
confidence: 99%
“…11). 147 The authors rationalized the result in terms of the better fitting of aromatic amino acid residues inside the bCD cavity, favoring the formation of poly(Mal-bCD):protein inclusion complexes. Complexation was actually found to destabilize the native conformation of the protein, favouring a partially unfolded state.…”
mentioning
confidence: 96%
“…CyDs have been claimed to interact with hydrophobic residues exposed on protein surfaces and thereby to decrease the aggregation of proteins [22, 23]. We previously reported that SBE4- β -CyD inhibited the aggregation of bovine insulin in neutral solution, possibly due to the interaction of SBE4- β -CyD with aromatic side chain of insulin such as B26-tyrosine, A19-tyrosine, B1-phenylalanine, and B25-phenylalanine [17].…”
Section: Resultsmentioning
confidence: 99%