4.8 Article

SYNBIP: synthetic binding proteins for research, diagnosis and therapy

期刊

NUCLEIC ACIDS RESEARCH
卷 50, 期 D1, 页码 D560-D570

出版社

OXFORD UNIV PRESS
DOI: 10.1093/nar/gkab926

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资金

  1. Entrepreneurship and Innovation Support Plan for Chinese Overseas Students of Chongqing [cx2020127]
  2. Natural Science Foundation of Zhejiang Province [LR21H300001]
  3. National Natural Science Foundation of China [81872798, U1909208]
  4. Leading Talent of the `Ten Thousand Plan'-National High-Level Talents Special Support Plan of China
  5. `Double Top-Class' University Project [181201*194232101]
  6. Fundamental Research Fund for Central Universities [2018QNA7023, 2019CDYGYB005]
  7. Key R&D Program of Zhejiang Province [2020C03010]
  8. Alibaba-Zhejiang University Joint Research Center of Future Digital Healthcare
  9. Information Technology Center of Zhejiang University
  10. Alibaba Cloud

向作者/读者索取更多资源

The SYNBIP database provides comprehensive information on thousands of SBPs, illustrating their scaffolds, biophysical and functional properties, binding targets and applications, as well as enabling similarity search. This database serves as a valuable resource for future development of novel SBPs through experimental protein engineering and in-silico studies. The SYNBIP database is accessible without login requirement at both official and mirror sites.
The success of protein engineering and design has extensively expanded the protein space, which presents a promising strategy for creating next-generation proteins of diverse functions. Among these proteins, the synthetic binding proteins (SBPs) are smaller, more stable, less immunogenic, and better of tissue penetration than others, which make the SBP-related data attracting extensive interest from worldwide scientists. However, no database has been developed to systematically provide the valuable information of SBPs yet. In this study, a database named 'Synthetic Binding Proteins for Research, Diagnosis, and Therapy (SYNBIP)' was thus introduced. This database is unique in (a) comprehensively describing thousands of SBPs from the perspectives of scaffolds, biophysical & functional properties, etc.; (b) panoramically illustrating the binding targets & the broad application of each SBP and (c) enabling a similarity search against the sequences of all SBPs and their binding targets. Since SBP is a human-made protein that has not been found in nature, the discovery of novel SBPs relied heavily on experimental protein engineering and could be greatly facilitated by in-silico studies (such as AI and computational modeling). Thus, the data provided in SYNBIP could lay a solid foundation for the future development of novel SBPs. The SYNBIP is accessible without login requirement at both official (https://idrblab.org/synbip/) and mirror (http://synbip.idrblab.net/) sites.

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