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.