Bio

Alia is a Research Development Specialist for the Stanford Research Development Office under VPDoR. She has a PhD from Stanford Engineering and a passion for interdisciplinary research. Her work experience spans academia, government, and industry, and is built around alternative energy, climate and sustainability. She has worked directly with policy makers in California in both the legislative and regulatory arenas to further the state's ambitious climate and energy goals and has prepared successful applications for funding from a variety of agencies at the state and national level. In her role at the RDO, Alia supports faculty teams from across the University, with a focus on large, collaborative research proposals in the STEM fields and a particular emphasis on climate & sustainability research.

Education & Certifications

  • Ph.D., Stanford University, Materials Science & Engineering (2013)
  • M.S., Stanford University, Biological Sciences (2006)
  • B.A., Northwestern University, Integrated Science Program (2003)

Contact

  • Work
    alia.schoen@stanford.edu
    University - Staff Department: Research Development Office Position: Research Development Specialist

All Publications

  • Biotemplated synthesis of inorganic materials: An emerging paradigm for nanomaterial synthesis inspired by nature PROGRESS IN MATERIALS SCIENCE Krajina, B. A., Proctor, A. C., Schoen, A. P., Spakowitz, A. J., Heilshorn, S. C. 2018; 91: 1–23

    View details for DOI 10.1016/j.pmatsci.2017.08.001

    View details for Web of Science ID 000415780300001

  • Multi-Site Functionalization of Protein Scaffolds for Bimetallic Nanoparticle Templating ADVANCED FUNCTIONAL MATERIALS Huggins, K. N., Schoen, A. P., Arunagirinathan, M. A., Heilshorn, S. C. 2014; 24 (48): 7737-7744

    View details for DOI 10.1002/adfm.201402049

    View details for Web of Science ID 000346498900020

  • Rheology and simulation of 2-dimensional clathrin protein network assembly. Soft matter VanDersarl, J. J., Mehraeen, S., Schoen, A. P., Heilshorn, S. C., Spakowitz, A. J., Melosh, N. A. 2014; 10 (33): 6219-6227

    Abstract

    Clathrin is a three-legged protein complex that assembles into lattice structures on the cell membrane and transforms into fullerene-like cages during endocytosis. This dynamic structural flexibility makes clathrin an attractive building block for guided assembly. The assembly dynamics and the mechanical properties of clathrin protein lattices are studied using rheological measurements and theoretical modelling in an effort to better understand two dynamic processes: protein adsorption to the interface and assembly into a network. We find that percolation models for protein network formation are insufficient to describe clathrin network formation, but with Monte Carlo simulations we can describe the dynamics of network formation very well. Insights from this work can be used to design new bio-inspired nano-assembly systems.

    View details for DOI 10.1039/c4sm00025k

    View details for PubMedID 25012232

  • Tuning colloidal association with specific peptide interactions SOFT MATTER Schoen, A. P., Hommersom, B., Heilshorn, S. C., Leunissen, M. E. 2013; 9 (29): 6781-6785

    View details for DOI 10.1039/c3sm50230a

    View details for Web of Science ID 000321273000023

  • Engineered clathrin nanoreactors provide tunable control over gold nanoparticle synthesis and clustering JOURNAL OF MATERIALS CHEMISTRY B Schoen, A. P., Huggins, K. N., Heilshorn, S. C. 2013; 1 (48): 6662-6669

    Abstract

    The use of biomolecules to direct nanomaterial synthesis has been an area of growing interest due to the complexity of structures that can be achieved in naturally occurring systems. We previously reported the functionalization of self-assembled clathrin protein cages to enable synthesis of nanoparticles from a range of inorganic materials. Here, we investigate the ability of this engineered biomolecule complex to act as a tunable nanoreactor for the formation of different arrangements of gold nanoparticles in three dimensions. We find that self-assembled clathrin cages functionalized with engineered bi-functional peptides induce formation of gold nanoparticles to generate solutions of either dispersed or clustered gold nanoparticles on demand. The 3D arrangement of nanoparticles is dependent on the concentration of the engineered peptide, which fulfills multiple roles in the synthesis process including stabilization of the nanoparticle surface and localization of the nanoparticles within the self-assembled clathrin cage. We propose and evaluate a mechanism that allows us to predict the peptide concentration at which the nanoreactor behavior switches. This work provides insight into peptide-based surfactants and the potential for incorporating them into strategies for tuning biological mineralization processes in mild solution conditions to generate complex structures.

    View details for DOI 10.1039/c3tb21145b

    View details for Web of Science ID 000327499100010

  • Dynamic remodelling of disordered protein aggregates is an alternative pathway to achieve robust self-assembly of nanostructures SOFT MATTER Schoen, A. P., Cordella, N., Mehraeen, S., Arunagirinathan, M. A., Spakowitz, A. J., Heilshorn, S. C. 2013; 9 (38): 9137-9145

    View details for DOI 10.1039/c3sm50830g

    View details for Web of Science ID 000324423700012

  • Engineered Protein Templates Synthesize Inorganic Nanomaterials CHEMICAL ENGINEERING PROGRESS Schoen, A. P., Schoen, D. T., Huggins, K. N., Adhimoolam, A. M., Heilshorn, S. C. 2012; 108 (12): 47-50

    View details for Web of Science ID 000312283600020

  • Molecular recognition enables biotemplating at distinct protein sites Huggins, K. N., Schoen, A. P., Arunagirinathan, M. A., Heilshorn, S. C. AMER CHEMICAL SOC. 2012

    View details for Web of Science ID 000324503203830

  • Self-assembly of Clathrin protein nanostructures Arunagirinathan, M., Gibbons, B. J., Schoen, A. P., Huggins, K. L., Heilshorn, S. C. AMER CHEMICAL SOC. 2012

    View details for Web of Science ID 000324475104134

  • Template Engineering Through Epitope Recognition: A Modular, Biomimetic Strategy for Inorganic Nanomaterial Synthesis JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Schoen, A. P., Schoen, D. T., Huggins, K. N., Arunagirinathan, M. A., Heilshorn, S. C. 2011; 133 (45): 18202-18207

    Abstract

    Natural systems often utilize a single protein to perform multiple functions. Control over functional specificity is achieved through interactions with other proteins at well-defined epitope binding sites to form a variety of functional coassemblies. Inspired by the biological use of epitope recognition to perform diverse yet specific functions, we present a Template Engineering Through Epitope Recognition (TEThER) strategy that takes advantage of noncovalent, molecular recognition to achieve functional versatility from a single protein template. Engineered TEThER peptides span the biologic-inorganic interface and serve as molecular bridges between epitope binding sites on protein templates and selected inorganic materials in a localized, specific, and versatile manner. TEThER peptides are bifunctional sequences designed to noncovalently bind to the protein scaffold and to serve as nucleation sites for inorganic materials. Specifically, we functionalized identical clathrin protein cages through coassembly with designer TEThER peptides to achieve three diverse functions: the bioenabled synthesis of anatase titanium dioxide, cobalt oxide, and gold nanoparticles in aqueous solvents at room temperature and ambient pressure. Compared with previous demonstrations of site-specific inorganic biotemplating, the TEThER strategy relies solely on defined, noncovalent interactions without requiring any genetic or chemical modifications to the biomacromolecular template. Therefore, this general strategy represents a mix-and-match, biomimetic approach that can be broadly applied to other protein templates to achieve versatile and site-specific heteroassemblies of nanoscale biologic-inorganic complexes.

    View details for DOI 10.1021/ja204732n

    View details for Web of Science ID 000297381200043

    View details for PubMedID 21967307

  • High Speed Water Sterilization Using One-Dimensional Nanostructures NANO LETTERS Schoen, D. T., Schoen, A. P., Hu, L., Kim, H. S., Heilshorn, S. C., Cui, Y. 2010; 10 (9): 3628-3632

    Abstract

    The removal of bacteria and other organisms from water is an extremely important process, not only for drinking and sanitation but also industrially as biofouling is a commonplace and serious problem. We here present a textile based multiscale device for the high speed electrical sterilization of water using silver nanowires, carbon nanotubes, and cotton. This approach, which combines several materials spanning three very different length scales with simple dying based fabrication, makes a gravity fed device operating at 100000 L/(h m(2)) which can inactivate >98% of bacteria with only several seconds of total incubation time. This excellent performance is enabled by the use of an electrical mechanism rather than size exclusion, while the very high surface area of the device coupled with large electric field concentrations near the silver nanowire tips allows for effective bacterial inactivation.

    View details for DOI 10.1021/nl101944e

    View details for Web of Science ID 000281498200068

    View details for PubMedID 20726518

  • Slm1 and Slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease MOLECULAR AND CELLULAR BIOLOGY Bultynck, G., Heath, V. L., Majeed, A. P., Galan, J., Haguenauer-Tsapis, R., Cyert, M. S. 2006; 26 (12): 4729-4745

    Abstract

    The Ca2+/calmodulin-dependent phosphatase calcineurin promotes yeast survival during environmental stress. We identified Slm1 and Slm2 as calcineurin substrates required for sphingolipid-dependent processes. Slm1 and Slm2 bind to calcineurin via docking sites that are required for their dephosphorylation by calcineurin and are related to the PXIXIT motif identified in NFAT. In vivo, calcineurin mediates prolonged dephosphorylation of Slm1 and Slm2 during heat stress, and this response can be mimicked by exogenous addition of the sphingoid base phytosphingosine. Slm proteins also promote the growth of yeast cells in the presence of myriocin, an inhibitor of sphingolipid biosynthesis, and regulation of Slm proteins by calcineurin is required for their full activity under these conditions. During heat stress, sphingolipids signal turnover of the uracil permease, Fur4. In cells lacking Slm protein activity, stress-induced endocytosis of Fur4 is blocked, and Fur4 accumulates at the cell surface in a ubiquitinated form. Furthermore, cells expressing a version of Slm2 that cannot be dephosphorylated by calcineurin display an increased rate of Fur4 turnover during heat stress. Thus, calcineurin may modulate sphingolipid-dependent events through regulation of Slm1 and Slm2. These findings, in combination with previous work identifying Slm1 and Slm2 as targets of Mss4/phosphatidylinositol 4,5-bisphosphate and TORC2 signaling, suggest that Slm proteins integrate information from a variety of signaling pathways to coordinate the cellular response to heat stress.

    View details for DOI 10.1128/MCB.01973-05

    View details for Web of Science ID 000238143100029

    View details for PubMedID 16738335

    View details for PubMedCentralID PMC1489119