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Article

Expanding Canonical Spider Silk Properties through a DNA Combinatorial Approach

1
Department of Biomedical Engineering, Tufts University, 4 Colby St, Medford, MA 02155, USA
2
School of Medicine, Boston University, Boston, MA 02118, USA
3
National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, Suzhou 215123, China
4
Department of Biological Engineering, Massachusetts Institute of Technology, 21 Ames St #56-651, Cambridge, MA 02142, USA
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Department of Process Development, Akouos Inc., 645 Summer St. Boston, MA 02210, USA
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Division of Innovation, Partners HealthCare Innovation, 215 First Street, Cambridge, MA 02142, USA
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Department of Research Solutions North America, MilliporeSigma, 400 Summit Dr, Burlington, MA 01803, USA
8
Department of Biological Science, University of Massachusetts Lowell, 198 Riverside Street, Olsen Hall 234, Lowell, MA 01854, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Materials 2020, 13(16), 3596; https://doi.org/10.3390/ma13163596
Received: 6 July 2020 / Revised: 9 August 2020 / Accepted: 10 August 2020 / Published: 14 August 2020
(This article belongs to the Special Issue Silk-Based Biomaterials)
The properties of native spider silk vary within and across species due to the presence of different genes containing conserved repetitive core domains encoding a variety of silk proteins. Previous studies seeking to understand the function and material properties of these domains focused primarily on the analysis of dragline silk proteins, MaSp1 and MaSp2. Our work seeks to broaden the mechanical properties of silk-based biomaterials by establishing two libraries containing genes from the repetitive core region of the native Latrodectus hesperus silk genome (Library A: genes masp1, masp2, tusp1, acsp1; Library B: genes acsp1, pysp1, misp1, flag). The expressed and purified proteins were analyzed through Fourier Transform Infrared Spectrometry (FTIR). Some of these new proteins revealed a higher portion of β-sheet content in recombinant proteins produced from gene constructs containing a combination of masp1/masp2 and acsp1/tusp1 genes than recombinant proteins which consisted solely of dragline silk genes (Library A). A higher portion of β-turn and random coil content was identified in recombinant proteins from pysp1 and flag genes (Library B). Mechanical characterization of selected proteins purified from Library A and Library B formed into films was assessed by Atomic Force Microscopy (AFM) and suggested Library A recombinant proteins had higher elastic moduli when compared to Library B recombinant proteins. Both libraries had higher elastic moduli when compared to native spider silk proteins. The preliminary approach demonstrated here suggests that repetitive core regions of the aforementioned genes can be used as building blocks for new silk-based biomaterials with varying mechanical properties. View Full-Text
Keywords: biomaterials; recombinant spider silk; broadening silk properties biomaterials; recombinant spider silk; broadening silk properties
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MDPI and ACS Style

Jaleel, Z.; Zhou, S.; Martín-Moldes, Z.; Baugh, L.M.; Yeh, J.; Dinjaski, N.; Brown, L.T.; Garb, J.E.; Kaplan, D.L. Expanding Canonical Spider Silk Properties through a DNA Combinatorial Approach. Materials 2020, 13, 3596. https://doi.org/10.3390/ma13163596

AMA Style

Jaleel Z, Zhou S, Martín-Moldes Z, Baugh LM, Yeh J, Dinjaski N, Brown LT, Garb JE, Kaplan DL. Expanding Canonical Spider Silk Properties through a DNA Combinatorial Approach. Materials. 2020; 13(16):3596. https://doi.org/10.3390/ma13163596

Chicago/Turabian Style

Jaleel, Zaroug, Shun Zhou, Zaira Martín-Moldes, Lauren M. Baugh, Jonathan Yeh, Nina Dinjaski, Laura T. Brown, Jessica E. Garb, and David L. Kaplan 2020. "Expanding Canonical Spider Silk Properties through a DNA Combinatorial Approach" Materials 13, no. 16: 3596. https://doi.org/10.3390/ma13163596

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