News Releases & Research Results Ultra-stable artificial protein retaining its folding ability even with loosened hydrophobic packing

The results of collaborative research conducted by Specially Appointed Researcher Rie Koga, graduate student Mami Yamamoto, Assistant Professor Takahiro Kosugi, and Associate Professor Nobuyasu Koga of the Protein Design Group, Research Center for Integrative Molecular Systems/Exploratory Research Center on Life and Living Systems, Institute for Molecular Science, Senior Fellow Naohiro Kobayashi of RIKEN SPring-8 Center, and Specially Appointed Assistant Professor Toshihiko Sugiki and Professor Toshimichi Fujiwara of the Institute for Protein Research, Osaka University.

• Artificial proteins designed so far were demonstrated to retain their folding ability and high thermal stability even after the loss of tight hydrophobic packing within their structures.
• Specifically, even if the hydrophobic amino acids responsible for packing were replaced with small hydrophobic amino acids (Val) of various sizes, the artificial protein retained its folding ability with a high denaturation temperature (>100^oC).
• The results of this research project should facilitate the development of technologies for thermostabilizing natural proteins or generating novel functional proteins through modifications of main-chain structures.

This project was conducted with the support of the Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS) by AMED.

The results were published online in the academic journal Proceedings of the National Academy of Sciences of the United States of America on November 24.

Koga R., et al. Robust folding of a de novo designed ideal protein even with most of the core mutated to valine PNAS
DOI: 10.1073/pnas.2002120117