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Contribution of lysine-containing cationic domains to thermally-induced phase transition of elastin-like proteins and their sensitivity to different stimuli
- Title
- Contribution of lysine-containing cationic domains to thermally-induced phase transition of elastin-like proteins and their sensitivity to different stimuli
- Authors
- Jeon, WB[Jeon, Won Bae]
- DGIST Authors
- Jeon, WB[Jeon, Won Bae]
- Issue Date
- 2011-01-31
- Citation
- BMB Reports, 44(1), 22-27
- Type
- Article
- Article Type
- Article
- Keywords
- Amino Acid Sequence; Biopolymer; Biopolymers; Cationic Diblock Biopolymers; Chemical Phenomena; Chemistry; Elastin; Elastin-Like Proteins; Extracellular Matrix Proteins; Hydrogen-Ion Concentration; Hydrophobic And Hydrophilic Interactions; Inorganic Salt; Intelligent Biomaterials; Inverse Phase Transition; Lysine; Metabolism; Micellar Assembly; Molecular Genetics; Molecular Sequence Data; pH; Phase Transition; Protein Structure, Tertiary; Protein Tertiary Structure; Salts; Scleroprotein; Temperature; Tropoelastin
- ISSN
- 1976-6696
- Abstract
- A series of elastin-like proteins, SKGPG[V(VKG)3VKVPG]n-(ELP1-90)WP (n = 1, 2, 3, and 4), were biosynthesized based on the hydrophobic and lysine linkage domains of tropoelastin. The formation of self-assembled hydrophobic aggregates was monitored in order to determine the influence of cationic segments on phase transition properties as well as the sensitivity to changes in salt and pH. The thermal transition profiles of the proteins fused with only one or two cationic blocks (n = 1 or 2) were similar to that of the counterpart ELP1-90. In contrast, diblock proteins that contain 3 and 4 cationic blocks displayed a triphasic profile and no transition, respectively. Upon increasing the salt concentration and pH, a stimulus-induced phase transition from a soluble conformation to an insoluble aggregate was observed. The effects of cationic segments on the stimuli sensitivity of cationic bimodal ELPs were interpreted in terms of their structural and molecular characteristics.
- URI
- http://hdl.handle.net/20.500.11750/3462
- DOI
- 10.5483/BMBRep.2011.44.1.22
- Publisher
- Korean Society for Molecular and Cellular Biology
- Related Researcher
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- Files:
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- Collection:
- Companion Diagnostics and Medical Technology Research Group1. Journal Articles
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