Biomimetic Production of Silk-Like Recombinant Squid Sucker Ring Teeth Proteins

被引:47
作者
Ding, Dawei [1 ]
Guerette, Paul A. [1 ,2 ]
Hoon, Shawn [3 ,4 ]
Kone, Kiat Whye [3 ]
Cornvik, Tobias [4 ]
Nilsson, Martina [4 ]
Kumar, Akshita [4 ]
Lescar, Julien [4 ]
Miserez, Ali [1 ,4 ]
机构
[1] Nanyang Technol Univ, Sch Mat Sci & Engn, Singapore 639798, Singapore
[2] Nanyang Technol Univ, Nanyang Technol Univ ERI N, Energy Res Inst, Singapore 637553, Singapore
[3] ASTAR, Inst Biomed Sci, Mol Engn Lab, Singapore 138673, Singapore
[4] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore
基金
新加坡国家研究基金会;
关键词
SPIDER DRAGLINE SILK; ESCHERICHIA-COLI; BIOLOGICAL-MATERIALS; ABRASION RESISTANCE; DRUG-DELIVERY; AFFINITY TAGS; FIBROIN; EXPRESSION; PURIFICATION; DESIGN;
D O I
10.1021/bm500670r
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The sucker ring teeth (SRT) of Humboldt squid exhibit mechanical properties that rival those of robust engineered synthetic polymers. Remarkably, these properties are achieved without a mineral phase or covalent cross-links. Instead, SRT are exclusively made of silk-like proteins called "suckerins", which assemble into nanoconfined beta-sheet reinforced suprarnolecular networks. In this study, three streamlined strategies for full-length recombinant suckerin protein production and purification were developed. Recombinant suckerin exhibited high solubility and colloidal stability in aqueous-based solvents. In addition, the colloidal suspensions exhibited a concentration-dependent conformational switch, from random coil to beta-sheet enriched structures. Our results demonstrate that recombinant suckerin can be produced in a facile manner in E. coli and processed from mild aqueous solutions into materials enriched in beta-sheets. We suggest that recombinant suckerin-based materials offer potential for a range of biomedical and engineering applications.
引用
收藏
页码:3278 / 3289
页数:12
相关论文
共 63 条
[1]   Wear and abrasion resistance selection maps of biological materials [J].
Amini, Shahrouz ;
Miserez, Ali .
ACTA BIOMATERIALIA, 2013, 9 (08) :7895-7907
[2]   Purification and characterization of recombinant spider silk expressed in Escherichia coli [J].
Arcidiacono, S ;
Mello, C ;
Kaplan, D ;
Cheley, S ;
Bayley, H .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1998, 49 (01) :31-38
[3]   Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins [J].
Arnau, Jos ;
Lauritzen, Conni ;
Petersen, Gitte E. ;
Pedersen, John .
PROTEIN EXPRESSION AND PURIFICATION, 2006, 48 (01) :1-13
[4]   Engineering protein thermostability using a generic activity-independent biophysical screen inside the cell [J].
Asial, Ignacio ;
Cheng, Yue Xiang ;
Engman, Henrik ;
Dollhopf, Maria ;
Wu, Binghuang ;
Nordlund, Par ;
Cornvik, Tobias .
NATURE COMMUNICATIONS, 2013, 4
[5]   Blueprint for a High-Performance Biomaterial: Full-Length Spider Dragline Silk Genes [J].
Ayoub, Nadia A. ;
Garb, Jessica E. ;
Tinghitella, Robin M. ;
Collin, Matthew A. ;
Hayashi, Cheryl Y. .
PLOS ONE, 2007, 2 (06)
[6]   What vibrations tell us about proteins [J].
Barth, A ;
Zscherp, C .
QUARTERLY REVIEWS OF BIOPHYSICS, 2002, 35 (04) :369-430
[7]   Mineral minimization in nature's alternative teeth [J].
Broomell, Christopher C. ;
Khan, Rashda K. ;
Moses, Dana N. ;
Miserez, Ali ;
Pontin, Michael G. ;
Stucky, Galen D. ;
Zok, Frank W. ;
Waite, J. Herbert .
JOURNAL OF THE ROYAL SOCIETY INTERFACE, 2007, 4 (12) :19-31
[8]   GENETIC-ENGINEERING OF STRUCTURAL PROTEIN POLYMERS [J].
CAPPELLO, J ;
CRISSMAN, J ;
DORMAN, M ;
MIKOLAJCZAK, M ;
TEXTOR, G ;
MARQUET, M ;
FERRARI, F .
BIOTECHNOLOGY PROGRESS, 1990, 6 (03) :198-202
[9]   Hyperspectral imaging of cuttlefish camouflage indicates good color match in the eyes of fish predators [J].
Chiao, Chuan-Chin ;
Wickiser, J. Kenneth ;
Allen, Justine J. ;
Genter, Brock ;
Hanlon, Roger T. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (22) :9148-9153
[10]  
Collins T., 2014, E COLI BIOMACROMOLEC