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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 SequenceBiopolymerBiopolymersCationic Diblock BiopolymersChemical PhenomenaChemistryElastinElastin-Like ProteinsExtracellular Matrix ProteinsHydrogen-Ion ConcentrationHydrophobic And Hydrophilic InteractionsInorganic SaltIntelligent BiomaterialsInverse Phase TransitionLysineMetabolismMicellar AssemblyMolecular GeneticsMolecular Sequence DatapHPhase TransitionProtein Structure, TertiaryProtein Tertiary StructureSaltsScleroproteinTemperatureTropoelastin
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
Files:
Collection:
Companion Diagnostics and Medical Technology Research Group1. Journal Articles


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