期刊
ACTA BIOMATERIALIA
卷 50, 期 -, 页码 322-333出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.actbio.2016.12.052
关键词
Bombyx mori silk fibroin; Fiber; Film; H-2 NMR relaxation; C-13 DD/MAS NMR
资金
- Ministry of Education, Science, Culture and Supports of Japan [25620169, 26248050]
- Impulsing Paradigm Change through Disruptive Technologies Program (ImPACT)
- National Institute of General Medical Sciences [SC1GM086268-09]
- Grants-in-Aid for Scientific Research [26248050] Funding Source: KAKEN
The mechanical properties of Bombyx mori silk fibroin (SF), such as elasticity and tensile strength, change remarkably upon hydration. However, the microscopic interaction with water is not currently well understood on a molecular level. In this work, the dynamics of water molecules interacting with SF was studied by H-2 solution NMR relaxation and exchange measurements. Additionally, the conformations of hydrated [3-C-13]Ala-, [3-C-13]Ser-, and [3-C-13]Tyr-SF fibers and films were investigated by C-13 DD/MAS NMR. Using an inverse Laplace transform algorithm, we were able to identify four distinct components in the relaxation times for water in SF fiber. Namely, A: bulk water outside the fiber, B: water molecules trapped weakly on the surface of the fiber, C: bound water molecules located in the inner surface of the fiber, and D: bound water molecules located in the inner part of the fiber were distinguishable. In addition, four components were also observed for water in the SF film immersed in methanol for 30 s, while only two components for the film immersed in methanol for 24 h. The effects of hydration on the conformation of Ser and Tyr residues in the site-specific crystalline and non-crystalline domains of C-13 selectively labeled SF, respectively, could be determined independently. Our measurements provide new insight relating the characteristics of water and the hydration structure of silk, which are relevant in light of current interest in the design of novel silk-based biomaterials. Statements of Significance The mechanical properties of Bombyx mori silk fibroin (SF) change remarkably upon hydration. However, the microscopic interaction between SF and water is not currently well understood on a molecular level. We were able to identify four distinct components in the relaxation times for water in SF fiber by H-2 solution NMR relaxation and exchange measurements. In addition, the effects of hydration on the conformation of Ser and Tyr residues in the site-specific crystalline and non-crystalline domains of C-13 selectively labeled SF, respectively, could be determined independently. Thus, our measurements provide new insight relating the characteristics of water and the hydration structure of silk, which are relevant in light of current interest in the design of novel silk-based biomaterials. (C) 2016 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
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