After receiving his Ph.D. at Prof. Yigong Shi’s Laboratory in Tsinghua University in 2014, Peilong Lu spent four and a half years at the University of Washington (UW) to design proteins that never existed in nature, based on the principles of biophysics and biochemistry, aided by computer simulation.
He has dealt with protein structures for 11 years.
At Tsinghua, he investigated the structure and function of membrane proteins. At UW, he explored de novo design of proteins with Prof. David Baker, director of the Institute for Protein Design. By simulating the interaction of protein polar residues in the membrane environment, he accurately designed the first three-dimensional structure of multi-pass transmembrane proteins in the world, proving that designer membrane proteins can spontaneously fold into structures consistent with the design models. The study published in Science paves the way for the design of multi-span transmembrane proteins with new functions, such as membrane receptors, channels, or antigen presenting scaffolds.
Peilong Lu is working on the design of transmembrane nanopores and ion channels with specific selectivity for different ions.
Transmembrane nanopores are the key molecule in nanopore DNA sequencing technology, which still needs to be improved for accuracy and stability. Therefore, de novo designed nanopores may provide an ideal solution for nanopore DNA sequencing, with custom defined shapes and chemical compositions for the recognition of DNA. Peilong Lu has made a significant breakthrough in this project, and a relevant manuscript is now under peer review.
In 2019, Peilong Lu started a laboratory at Westlake University to continue his research on membrane protein design. He is ready to explore more and turn his imagination into reality.