The molecular conformation of silk fibroin regulates osteogenic cell behavior by modulating the stability of the adsorbed protein-material interface

Yanlin Long; Xian Cheng; John A.Jansen; Sander G.C.Leeuwenburgh; Jing Mao; Fang Yang; Lili Chen

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The molecular conformation of silk fibroin regulates osteogenic cell behavior by modulating the stability of the adsorbed protein-material interface

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Silk fibroin(SF)can be used to construct various stiff material interfaces to support bone formation.An essential preparatory step is to partially transform SF molecules from random coils toβ-sheets to render the material water insoluble.However,the influence of the SF conformation on osteogenic cell behavior at the material interface remains unknown.Herein,three stiff SF substrates were prepared by varying theβ-sheet content(high,medium,and low).The substrates had a comparable chemical composition,surface topography,and wettability.When adsorbed fibronectin was used as a model cellular adhesive protein,the stability of the adsorbed protein-material interface,in terms of the surface stability of the SF substrates and the accompanying fibronectin detachment resistance,increased with the increasingβ-sheet content of the SF substrates.Furthermore,(i)larger areas of cytoskeleton-associated focal adhesions,(ii)higher orders of cytoskeletal organization and(iii)more elongated cell spreading were observed for bone marrow-derived mesenchymal stromal cells(BMSCs)cultured on SF substrates with high vs.lowβ-sheet contents,along with enhanced nuclear translocation and activation of YAP/TAZ and RUNX2.Consequently,osteogenic differentiation of BMSCs was stimulated on highβ-sheet substrates.These results indicated that theβ-sheet content influences osteogenic differentiation of BMSCs on SF materials in vitro by modulating the stability of the adsorbed protein-material interface,which proceeds via protein-focal adhesion-cytoskeleton links and subsequent intracellular mechanotransduction.Our findings emphasize the role of the stability of the adsorbed protein-material interface in cellular mechanotransduction and the perception of stiff SF substrates with differentβ-sheet contents,which should not be overlooked when engineering stiff biomaterials.

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《骨研究：英文》 |2021年第2期|P.188-199|共12页
作者
Yanlin Long; Xian Cheng; John A.Jansen; Sander G.C.Leeuwenburgh; Jing Mao; Fang Yang; Lili Chen;
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作者单位

Department of Stomatology Union Hospital Tongji Medical College Huazhong University of Science and Technology Wuhan 430022 ChinaHubei Province Key Laboratory of Oral and Maxillofacial Development and Regeneration Wuhan 430022 China;

Department of Dentistry–Biomaterials Radboud University Medical Center Philips van Leydenlaan 25 6525 EX Nijmegen The Netherlands;

Department of Dentistry–Biomaterials Radboud University Medical Center Philips van Leydenlaan 25 6525 EX Nijmegen The Netherlands;

Department of Dentistry–Biomaterials Radboud University Medical Center Philips van Leydenlaan 25 6525 EX Nijmegen The Netherlands;

Center of Stomatology Tongji Hospital Tongji Medical College Huazhong University of Science and Technology Wuhan 430030 China;

Department of Dentistry–Biomaterials Radboud University Medical Center Philips van Leydenlaan 25 6525 EX Nijmegen The Netherlands;

Department of Stomatology Union Hospital Tongji Medical College Huazhong University of Science and Technology Wuhan 430022 ChinaHubei Province Key Laboratory of Oral and Maxillofacial Development and Regeneration Wuhan 430022 China;

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原文格式 PDF
正文语种 chi
中图分类金属学与热处理;
关键词
interface; stability; adsorbed;

The molecular conformation of silk fibroin regulates osteogenic cell behavior by modulating the stability of the adsorbed protein-material interface

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