Tuning a coiled-coil hydrogel via computational design of supramolecular fiber assembly

被引:7
|
作者
Britton, Dustin [1 ]
Meleties, Michael [1 ]
Liu, Chengliang [1 ]
Jia, Sihan [1 ]
Mahmoudinobar, Farbod [1 ,2 ]
Renfrew, P. Douglas [2 ]
Bonneau, Richard [2 ,3 ,4 ]
Montclare, Jin Kim [1 ,5 ,6 ,7 ]
机构
[1] NYU, Tandon Sch Engn, Dept Chem & Biomol Engn, Brooklyn, NY 11201 USA
[2] Simons Fdn, Ctr Computat Biol, Flatiron Inst, New York, NY 10010 USA
[3] NYU, Ctr Genom & Syst Biol, New York, NY 10003 USA
[4] NYU, Courant Inst Math Sci, Comp Sci Dept, New York, NY 10009 USA
[5] NYU, Sch Med, Bernard & Irene Schwartz Ctr Biomed Imaging, Dept Radiol, New York, NY 10016 USA
[6] NYU, Dept Chem, New York, NY 10012 USA
[7] NYU, Coll Dent, Dept Biomat, New York, NY 10010 USA
来源
关键词
PROTEIN; PEPTIDE; GELATION; DEGRADATION; SECONDARY;
D O I
10.1039/d2me00153e
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The previously reported Q is a thermoresponsive coiled-coil protein capable of higher-order supramolecular assembly into fibers and hydrogels with upper critical solution temperature (UCST) behavior. Here, we introduce a new coiled-coil protein that is redesigned to disfavor lateral growth of its fibers and thus achieve a higher crosslinking density within the formed hydrogel. We also introduce a favorable hydrophobic mutation to the pore of the coiled-coil domain for increased thermostability of the protein. We note that an increase in storage modulus of the hydrogel and crosslinking density is coupled with a decrease in fiber diameter. We further fully characterize our alpha-helical coiled-coil (Q2) hydrogel for its structure, nano-assembly, and rheology relative to our previous single domain protein, Q, over the time of its gelation demonstrating the nature of our hydrogel self-assembly system. In this vein, we also characterize the ability of Q2 to encapsulate the small hydrophobic small molecule, curcumin, and its impact on the mechanical properties of Q2. The design parameters here not only show the importance of electrostatic potential in self-assembly but also provide a step towards predictable design of electrostatic protein interactions.
引用
收藏
页码:217 / 226
页数:10
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