Recombinant Silk Fibroin Crystalline Regions as Biomaterial Alternatives to the Full-Length Protein

Zifan Wang; Bogdan A. Serban; Monica A. Serban

doi:10.1021/acsbiomaterials.0c01103

Recombinant Silk Fibroin Crystalline Regions as Biomaterial Alternatives to the Full-Length Protein

Zifan Wang
, Bogdan A. Serban
, Monica A. Serban

University of Montana

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Silk fibroin is a natural polymer with a unique repetitive structure that translates to extraordinary properties in terms of processability and mechanical properties. The Bombyx mori silk has a molecular weight of ∼415 kDa and consists of a light chain and a heavy chain. Its heavy chain is organized into 12 crystalline domains. Each of these crystalline domains contains subdomains of ∼70 amino acid containing blocks. It is well understood that the heavy chain of the protein is responsible for its processing versatility and excellent mechanical properties; however, the need for the high number of monomeric repeating units is unclear, and the individual properties of crystalline regions compared to those of the full-length protein are not understood. The work described herein assessed the possibility of using recombinant crystalline regions as alternative biomaterials for applications such as tissue adhesives. Our results indicate that while the two tested substructures do not fully recapitulate the native silk fibroin's properties, they appear to be a suitable alternative for the production of silk-based medical adhesives.

Original language	English
Pages (from-to)	7004-7010
Number of pages	7
Journal	ACS Biomaterials Science and Engineering
Volume	6
Issue number	12
DOIs	https://doi.org/10.1021/acsbiomaterials.0c01103
State	Published - Dec 14 2020

Funding

Funding for this project was provided by a pilot project grant from the Center for Biomolecular Structure and Dynamics COBRE, NIH Grant P20GM103546. We thank Dr. Tung-Chung Mou, Dr. Baisen Zeng, and Dr. Sascha Stump from the Center for Biomolecular Structure and Dynamics for their help with this project, and Dr. Stephen Sprang, Director of the Center for Biomolecular Structure and Dynamics, for his review of the manuscript and helpful discussions. We also thank Dr. Klara Briknarova from the University of Montana, Department of Chemistry and Biochemistry, for providing the human recombinant fibronectin monomer for the fluorescence spectroscopy studies. Funding for this project was provided by a pilot project grant from the Center for Biomolecular Structure and Dynamics COBRE, NIH Grant P20GM103546. We thank Dr. Tung-Chung Mou, Dr. Baisen Zeng, and Dr. Sascha Stump from the Center for Biomolecular Structure and Dynamics for their help with this project, and Dr. Stephen Sprang Director of the Center for Biomolecular Structure and Dynamics, for his review of the manuscript and helpful discussions. We also thank Dr. Klara Briknarova from the University of Montana, Department of Chemistry and Biochemistry, for providing the human recombinant fibronectin monomer for the fluorescence spectroscopy studies.

Funders	Funder number
Center for Biomolecular Structure and Dynamics
P20GM103546

Keywords

protein interactions
recombinant expression
silk fibroin
structural changes

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10.1021/acsbiomaterials.0c01103

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title = "Recombinant Silk Fibroin Crystalline Regions as Biomaterial Alternatives to the Full-Length Protein",

abstract = "Silk fibroin is a natural polymer with a unique repetitive structure that translates to extraordinary properties in terms of processability and mechanical properties. The Bombyx mori silk has a molecular weight of ∼415 kDa and consists of a light chain and a heavy chain. Its heavy chain is organized into 12 crystalline domains. Each of these crystalline domains contains subdomains of ∼70 amino acid containing blocks. It is well understood that the heavy chain of the protein is responsible for its processing versatility and excellent mechanical properties; however, the need for the high number of monomeric repeating units is unclear, and the individual properties of crystalline regions compared to those of the full-length protein are not understood. The work described herein assessed the possibility of using recombinant crystalline regions as alternative biomaterials for applications such as tissue adhesives. Our results indicate that while the two tested substructures do not fully recapitulate the native silk fibroin's properties, they appear to be a suitable alternative for the production of silk-based medical adhesives.",

keywords = "protein interactions, recombinant expression, silk fibroin, structural changes",

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T1 - Recombinant Silk Fibroin Crystalline Regions as Biomaterial Alternatives to the Full-Length Protein

AU - Wang, Zifan

AU - Serban, Bogdan A.

AU - Serban, Monica A.

PY - 2020/12/14

Y1 - 2020/12/14

N2 - Silk fibroin is a natural polymer with a unique repetitive structure that translates to extraordinary properties in terms of processability and mechanical properties. The Bombyx mori silk has a molecular weight of ∼415 kDa and consists of a light chain and a heavy chain. Its heavy chain is organized into 12 crystalline domains. Each of these crystalline domains contains subdomains of ∼70 amino acid containing blocks. It is well understood that the heavy chain of the protein is responsible for its processing versatility and excellent mechanical properties; however, the need for the high number of monomeric repeating units is unclear, and the individual properties of crystalline regions compared to those of the full-length protein are not understood. The work described herein assessed the possibility of using recombinant crystalline regions as alternative biomaterials for applications such as tissue adhesives. Our results indicate that while the two tested substructures do not fully recapitulate the native silk fibroin's properties, they appear to be a suitable alternative for the production of silk-based medical adhesives.

AB - Silk fibroin is a natural polymer with a unique repetitive structure that translates to extraordinary properties in terms of processability and mechanical properties. The Bombyx mori silk has a molecular weight of ∼415 kDa and consists of a light chain and a heavy chain. Its heavy chain is organized into 12 crystalline domains. Each of these crystalline domains contains subdomains of ∼70 amino acid containing blocks. It is well understood that the heavy chain of the protein is responsible for its processing versatility and excellent mechanical properties; however, the need for the high number of monomeric repeating units is unclear, and the individual properties of crystalline regions compared to those of the full-length protein are not understood. The work described herein assessed the possibility of using recombinant crystalline regions as alternative biomaterials for applications such as tissue adhesives. Our results indicate that while the two tested substructures do not fully recapitulate the native silk fibroin's properties, they appear to be a suitable alternative for the production of silk-based medical adhesives.

KW - protein interactions

KW - recombinant expression

KW - silk fibroin

KW - structural changes

UR - https://www.scopus.com/pages/publications/85096560788

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JF - ACS Biomaterials Science and Engineering

IS - 12

ER -

Recombinant Silk Fibroin Crystalline Regions as Biomaterial Alternatives to the Full-Length Protein

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Keywords

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