Bio

A public sector professional with a decade of experience leading climate equity programs and community outreach strategies, with a focus on environmental justice and improving health outcomes for underserved communities. Most recently served as Director of Community Strategies and Resources at the San Joaquin Valley Air Pollution Control District, where efforts were dedicated to addressing pollution in low-income communities.

Leveraged expertise in community outreach and budget management to develop impactful programs for vulnerable populations. Pursuing a Master of Science in Management at Stanford Graduate School of Business to explore innovative approaches in sustainable policy, climate technology, and the circular economy to advance global environmental justice.

Professional Affiliations and Activities

  • Investor, Justice, Stanford GSB Impact Fund (2025 - Present)

Education & Certifications

  • MS, UC Irvine, Biomedical Engineering (2014)
  • BS, UCLA, Bioengineering (2011)

Contact

  • Academic
    olsenj@stanford.edu
    University - Student Department: Graduate School of Business Position: Graduate, Business

Links

All Publications

  • Steric effects in peptide and protein exchange with activated disulfides. Biomacromolecules Kerr, J., Schlosser, J. L., Griffin, D. R., Wong, D. Y., Kasko, A. M. 2013; 14 (8): 2822-9

    Abstract

    Disulfide exchange is an important bioconjugation tool, enabling chemical modification of peptides and proteins containing free cysteines. We previously reported the synthesis of a macromer bearing an activated disulfide and its incorporation into hydrogels. Despite their ability to diffuse freely into hydrogels, larger proteins were unable to undergo in-gel disulfide exchange. In order to understand this phenomenon, we synthesized four different activated disulfide-bearing model compounds (Mn = 300 Da to 10 kDa) and quantified their rate of disulfide exchange with a small peptide (glutathione), a moderate-sized protein (β-lactoglobulin), and a large protein (bovine serum albumin) in four different pH solutions (6.0, 7.0, 7.4, and 8.0) to mimic biological systems. Rate constants of exchange depend significantly on the size and accessibility of the thiolate. pH also significantly affects the rate of reaction, with the faster reactions occurring at higher pH. Surprisingly, little difference in exchange rates is seen between macromolecular disulfides of varying size (Mn = 2 kDa - 10 kDa), although all undergo exchange more slowly than their small molecule analogue (MW = 300 g/mol). The maximum exchange efficiencies (% disulfides exchanged after 24 h) are not siginificantly affected by thiol size or pH, but somewhat affected by disulfide size. Therefore, while all three factors investigated (pH, disulfide size, and thiolate size) can influence the exchange kinetics and extent of reaction, the size of the thiolate and its accessibility plays the most significant role.

    View details for DOI 10.1021/bm400643p

    View details for PubMedID 23865598

    View details for PubMedCentralID PMC4198305

  • Synthesis of photodegradable macromers for conjugation and release of bioactive molecules. Biomacromolecules Griffin, D. R., Schlosser, J. L., Lam, S. F., Nguyen, T. H., Maynard, H. D., Kasko, A. M. 2013; 14 (4): 1199-207

    Abstract

    Hydrogel scaffolds are used in biomedicine to study cell differentiation and tissue evolution, where it is critical to control the delivery of chemical cues both spatially and temporally. While large molecules can be physically entrapped in a hydrogel, moderate molecular weight therapeutics must be tethered to the hydrogel network through a labile linkage to allow controlled release. We synthesized and characterized a library of polymerizable ortho-nitrobenzyl (o-NB) macromers with different functionalities at the benzylic position (alcohol, amine, BOC-amine, halide, acrylate, carboxylic acid, activated disulfide, N-hydroxysuccinyl ester, biotin). This library of polymerizable macromers containing o-NB groups should allow direct conjugation of nearly any type of therapeutic agent and its subsequent controlled photorelease from a hydrogel network. As proof-of-concept, we incorporated the N-hydroxysuccinyl ester macromer into hydrogels and then reacted phenylalanine with the NHS ester. Upon exposure to light (λ = 365 nm; 10 mW/cm(2), 10 min), 81.3% of the phenylalanine was released from the gel. Utilizing the photodegradable macromer incorporating an activated disulfide, we conjugated a cell-adhesive peptide (GCGYGRGDSPG), a protein that exhibits enzymatic activity (bovine serum albumin (BSA)), and a growth factor (transforming growth factor-β1 (TGF-β1)) into hydrogels, controlled their release with light (λ = 365 nm; 10 mW/cm(2), 0-20 min), and verified the bioactivity of the photoreleased molecules. The photoreleasable peptide allows real-time control over cell adhesion. BSA maintains full enzymatic activity upon sequestration and release from the hydrogel. Photoreleased TGF-β1 is able to induce chondrogenic differentiation of human mesenchymal stem cells comparable to native TGF-β1. Through this approach, we have demonstrated that photodegradable tethers can be used to sequester peptides and proteins into hydrogel depots and release them in an externally controlled, predictable manner without compromising biological function.

    View details for DOI 10.1021/bm400169d

    View details for PubMedID 23506440

    View details for PubMedCentralID PMC4198304