August 26, 2014
The Foldit community to targets Ebola. Click here to learn more.
Make a donation to help us fund our anti-Ebola effort.
The Foldit community to targets Ebola. Click here to learn more.
Make a donation to help us fund our anti-Ebola effort.
Watch a video documenting a recent hike at The Brothers in the Olympics.
IPD scientists, mountain goats, and stellar views – oh my!
Read a post about how the power of volunteer computing drives advances in protein design! Learn more at the link.
Read a letter from Institute for Protein Design Director Dr. David Baker summarizing the exciting accomplishments and progress made at the IPD in the past year.
This July, IPD staff and scientists ventured outdoors for a conference and for some fun adventures. Learn more at the link.
June at the IPD welcomed some new team members and saw some exciting new publications! Learn more here.
What if scientists could design a completely new protein that is precision-tuned to bind and inhibit cancer-causing proteins in the body? Collaborating scientists at the UW Institute for Protein Design (IPD) and Molecular Engineering and Sciences Institute (MolES) have made this idea a reality with the designed protein BINDI. BINDI (BHRF1-INhibiting Design acting Intracellularly) is a completely novel protein, based on a new protein scaffold not found in nature, and designed to bind BHRF1, a protein encoded by the Epstein-Barr virus (EBV) which is responsible for disregulating cell growth towards a cancerous state. Learn more here.
A new paper is out in the June 5 issue of Nature entitled Accurate design of co-assembling multi-component protein nanomaterials. Scientists at the Institute for Protein Design (IPD), in collaboration with researchers at UCLA and HHMI, have built upon their previous work constructing single-component protein nanocages and can now design and build self-assembling protein nanomaterials made up of multiple components with near atomic-level accuracy. Learn more about this innovative work at this link.
May was a busy month at the IPD, with some new publications and exciting announcements! Learn more here.
In a recent PNAS paper entitled “Removing T-cell epitopes with computational protein design”, IPD researchers combine machine learning with computational protein design to demonstrate immune silencing of protein targets. This deimmunization has the potential to reduce or eliminate immunogenicity of protein therapeutics. Learn more at this link.
A recent Nature issue exposed the dismaying fact that many women are deterred from pursuing a career in science, especially at the highest levels (postdoctoral positions, faculty position, scientific advisory boards to start up companies, etc). To talk about this significant gender gap in science and the issues female scientists face, Baker lab members participated in an informal lunch discussion to determine what specific steps could be taken as a group to encourage and promote women within our own scientific community. Learn more at this link.
With a very generous $8 M gift from the Washington Research Foundation (WRF), the IPD has launched the WRF-IPD Innovation Fellows Program supporting research partnerships between the IPD and other Seattle-area research institutes or UW departments. We are recruiting exceptionally talented researchers who have just finished their PhD to join expert laboratories at local institutions where they will apply protein design methods to current health, energy, and materials related research problems. For more information see our web page here.
The “Three Dreamers” are a group of Seattle-based philanthropists whose family members are suffering from Alzheimer’s disease (AD). The IPD has partnered with the Three Dreamers, the Foldit community and AD researchers at the UW to design new proteins targeting amyloid, thought to be the cause of AD. Learn more at this link.
Re/Code writer James Temple has written an interesting article on David Baker’s efforts to design a new world of proteins. The article covers the IPD efforts to design proteins that neutralize the flu virus, Alzheimer’s disease amyloid protein, and how the IPD is engaging citizen scientists in the Rosetta@home and Foldit projects. Learn more at this link.
Baker lab members published in Nature Chemical Biology a paper entitled “Design of activated serine-containing catalytic triads with atomic-level accuracy“, describing the computational design of proteins with idealized serine-containing catalytic triads which can capture and neutralize organophosphate probes. This work has utility in design of scavengers of environmental toxins. Learn more at this link.
Foldit is 5 years old. This publication entitled “Increasing public involvement in structural biology” chronicles the power of engaging the citizen science community on behalf of the computational challenge of protein folding. Learn more at this link.
What if scientists could design proteins to capture specific metals from our environment? The utility for cleaning up metals from waste water, soils, and our bodies could be tremendous. Dr. Jeremy Mills and collaborators in Dr. Baker’s group at the University of Washington’s Institute for Protein Design (IPD) address this challenge in the first reported use of computational protein design software, Rosetta, to engineer a new metal binding protein (“MB-07”) which incorporates an “unnatural amino acid” (UAA) to achieve very high affinity binding to metal cations. Learn more at this link.
In a widely cited Nature paper entitled Proof of principle for epitope-focused vaccine design, IPD researchers and collaborators invented a new method to design novel proteins for use as a candidate vaccines to protect against respiratory syncytial virus (RSV), a significant cause of infant mortality. Learn more at this link.
The Seattle Health Innovators recently visited the Institute for Protein Design, and wrote a nice blog entitled “Crowdsourcing the design of new molecules to improve healthcare and the environment.” The article provides a nice look into the Institute for Protein Design. Learn more at this link.
Purification of antibody IgG from crude serum or culture medium is required for virtually all research, diagnostic, and therapeutic antibody applications. Researchers at the Institute for Protein Design (IPD) have used computational methods to design a new protein (called “Fc-Binder”) that is programed to bind to the constant portion of IgG (aka “Fc” region) at basic pH (8.0) but to release the IgG at slightly acidic pH (5.5). Published on-line at PNAS (Dec. 31, 2013), the paper is entitled Computational design of a pH-sensitive IgG binding protein, co-authored by Strauch, E. – M., Fleishman S. J., & Baker D. Learn more at this link.
Dr. Ingrid Swanson Pultz, a Translational Investigator at the Institute for Protein Design won first prize at the UW Center for Commercialization 2013 Innovator Recognition Event, for KumaMax, an enzyme designed in the Baker lab to efficiently break down gluten within the acidic environment of the stomach, before it can reach the small intestine where intact gluten may otherwise cause an inflammatory reaction in people who suffer from celiac disease. Learn more at this link.
David Baker, Head of the Institute for Protein Design was recently in Toronto, Canada in late October to deliver a lecture on protein design as part of Gairdner Award celebrations. This was written up in the Globe and Mail. Learn more at this link.
Thank you to our supporters. GIVING IN ACTION: Making Dreams Come True.
Barton Family Foundation, Life Sciences Discovery Fund,
Bruce and Jeannie Nordstrom, and Three Dreamers all supporting the IPD.
Thank you all for your help in supporting our efforts in protein design.
V-type nerve agents are among the most toxic compounds known, and are chemically related to pesticides widespread in the environment. Using an integrated approach, described in an ACS Chemical Biology paper entitled Engineering V-type nerve agents detoxifying enzymes using computationally focused libraries, Dr. Izhack Cherny, Dr. Per Greisen, and collaborators increased the rate of nerve agent detoxification by the enzyme phosphotriesterase (PTE) by 5000-fold by redesigning the active site. Learn more at this link.
Prof. David Baker, Head of the UW Institute for Protein Design, HHMI Investigator provides an in depth discussion on the design of protein structures, functions and assemblies. Click here to watch the video.
Researchers in the Baker group describe an improved method for comparative modeling, RosettaCM, which optimizes a physically realistic all-atom energy function over the conformational space defined by homologous structures. Learn more at this link.
In a Journal of Molecular Biology publication entitled Computational design of a protein-based enzyme inhibitor, Dr. Erik Procko and collaborators describe the computational design of a protein-based enzyme inhibitor that binds the polar active site of hen egg lysosome (HEL). Computational design of a protein that binds polar surfaces has not been previously accomplished. Learn more at this link.
Brain cancer is a serious unmet medical challenge, and Washington state is one of the leading research clusters working on glioblastoma. Here we report on how RosettaDesign proteins are being used to treat brain cancer! Read more about this important translational protein design effort here.
The Life Sciences Discovery Fund (LSDF) today announced its latest round of Opportunity Grants, and awarded $1.4 M to the University of Washington (UW) to “Launch of the Institute for Protein Design for Creating New Therapeutics, Vaccines and Diagnostics.” This LSDF Opportunity Grant Award will enable the IPD Translational Investigators to improve upon protein design discoveries so that they may one day become viable solutions to real-life challenges. The LSDF funding is to be matched by contributions from UW and private donors (donations which can be made here). Lear more at this link.
Reported on-line in Nature (Sept. 4, 2013) researchers at the Institute for Protein Design describe the use of Rosetta computer algorithms to design a protein which binds with high affinity and specificity to a small drug molecule, digoxigenin a dangerous but sometimes life saving cardiac glycoside. Learn more at this link.
IPD researchers in the Baker group have published new computational protocols for preparing protein scaffold libraries for functional site design. Their paper entitled “A Pareto-optimal refinement method for protein design scaffolds“ improves the search for amino acids with the lowest energy subject to a set of constraints specifying function. Learn more at this link.
Dr. David Baker, Director of the IPD delivered the Centenary Award and Frederick Gowland Hopkins Memorial Lecture at at the MRC Laboratory of Molecular Biology, Cambridge, UK, on December, 13, 2012. Baker’s lecture entitled “Protein folding, structure prediction and design” can be read at this published link.
A team from David Baker’s laboratory at the University of Washington in Seattle have described a set of “rules” for the design of proteins from scratch, and have demonstrated the successful design of five new proteins that fold reliably into predicted conformations. Their work was published Nature. Learn more at this link.
The Institute for Protein Design and David Baker’s laboratory have moved into the new Molecular Engineering & Sciences Building located in the heart of the University of Washington campus. Read about the Institute’s new home and its exciting research in the Seattle Times, and also at this link.
As reported in Nature Biotechnology, David Baker and scientists at the IPD published exciting new methods to improve the potency and breadth of computer-designed protein inhibitors of influenza. Learn more at this link.
IPD researchers in the Baker group have published in Science a paper entitled “Computational design of self-assembling protein nanomaterials with atomic level accuracy.” They describe a general computational method for designing proteins that self-assemble to a desired symmetric architecture. Protein building blocks are docked together symmetrically to identify complementary packing arrangements, and low-energy protein-protein interfaces are then designed between the building blocks in order to drive self-assembly. Read more at this link.
Dr. Paul Ramsey, CEO of UW Medicine, announces the establishment of the Institute for Protein Design (IPD). “A major challenge for designing proteins for specific purposes is predicting three-dimensional shape from the amino acid sequence. Dr. David Baker, UW professor of biochemistry and an investigator of the Howard Hughes Medical Institute, has had remarkable success in making these predictions and in designing new proteins with new functions.”
Baker will serve as the director or the IPD which will coalesce and expand existing strengths within the UW and Seattle. The IPD will integrate UW expertise in biochemistry, engineering, computer science and medicine, and leverage local strength in the software industry to design a whole new world of synthetic proteins that address challenges in medicine, energy and technology.