TY - JOUR
T1 - Contribution of lysine-containing cationic domains to thermally-induced phase transition of elastin-like proteins and their sensitivity to different stimuli
AU - Jeon, Won Bae
PY - 2011/1
Y1 - 2011/1
N2 - 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.
AB - 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.
KW - Cationic diblock biopolymers
KW - Elastin-like proteins
KW - Intelligent biomaterials
KW - Inverse phase transition
KW - Micellar assembly
UR - http://www.scopus.com/inward/record.url?scp=79751505034&partnerID=8YFLogxK
U2 - 10.5483/BMBRep.2011.44.1.22
DO - 10.5483/BMBRep.2011.44.1.22
M3 - Article
C2 - 21266102
AN - SCOPUS:79751505034
SN - 1976-6696
VL - 44
SP - 22
EP - 27
JO - BMB Reports
JF - BMB Reports
IS - 1
ER -