Tuning Thermoresponsive Properties of Cationic Elastin-like Polypeptides by Varying Counterions and Side-Chains

被引:43
作者
Petitdemange, Rosine [1 ]
Garanger, Elisabeth [1 ]
Bataille, Laure [1 ]
Bathany, Katell [2 ]
Garbay, Bertrand [1 ]
Deming, Timothy J. [3 ,4 ]
Lecommandoux, Sebastien [1 ]
机构
[1] Univ Bordeaux Bordeaux INP, ENSCBP, CNRS, Lab Chim Polymeres Organ UMR5629, 16 Ave Pey Berland, F-33607 Pessac, France
[2] Univ Bordeaux Bordeaux INP, CNRS, Chim & Biol Membranes & Nano Objets UMR5248, Allee Geoffroy St Hilaire, F-33600 Pessac, France
[3] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
[4] Univ Calif Los Angeles, Dept Bioengn, Los Angeles, CA 90095 USA
基金
美国国家科学基金会;
关键词
PROTEIN-BASED POLYMERS; BIOMEDICAL APPLICATIONS; CANCER-THERAPY; DRUG-DELIVERY; POLYPENTAPEPTIDE; NANOPARTICLES; TRANSITION; PEPTIDES; BEHAVIOR; DESIGN;
D O I
10.1021/acs.bioconjchem.7b00082
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
We report the synthesis of methionine-containing recombinant elastin-like polypeptides (ELPs) of different lengths that contain periodically spaced methionine residues. These ELPs were chemoselectively alkylated at all methionine residues to give polycationic derivatives. Some of these samples were found to possess solubility transitions in water, where the temperature of these transitions varied with ELP concentration, nature of the methionine alkylating group, and nature of the sulfonium counterions. These studies show that introduction and controlled spacing of methionine sulfonium residues into ELPs can be used as a means both to tune their solubility transition temperatures in water using a variety of different parameters and to introduce new side-chain functionality.
引用
收藏
页码:1403 / 1412
页数:10
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