https://pages.htgaa.org/2026b/david-morales/index.htmlAbout me Hi! I’m David, a Junior year Biotechnology Engineering student from Universidad Mayor de San Simón, Cochabamba, Bolivia! ❤🇧🇴 When I was a child, I always wanted to become a phycist. Then I discovered synthetic biology. 🧬 I’m a curious observer of the universe, of the tiny persistent reminders that we are the universe experiencing itself through endless cycles of order and disorder. I find beauty in describing, but also experiencing universe by ourselves. I’m fascinated with thermodynamics, the origin of life, complexity science and chaos theory. The last one is the craziest one, as it is related with quantum physics, DNA expression, genetics, evolution, information science, inferential statistics and more! I’m paraphrasing Stephen Hawking: “We don’t dare to ask the big questions as much as we should.” I do dare. Some of the biggest questions driving me are: Why and how are we conscious? What makes us human? Does life have any inherent meaning? (obviously, all of them from the scientific perspective). I’m in search for answers. 🧠 I’m very interested in systems biology because it is a powerful approach to understand the brain and the consciousness thing. In the coming years, I plan to apply to a Neuroscience PhD program, where I hope to contribute to unraveling these mysteries at the frontier of neuroscience, computation, and physics. ❤Hugoenhttps://pages.htgaa.org/2026b/david-morales/week-01-hw-project-ideas/index.htmlMon, 01 Jan 0001 00:00:00 +0000https://pages.htgaa.org/2026b/david-morales/week-01-hw-project-ideas/index.html1. What do you want to make? I want to biomanufacture a pair of orthogonal synthetic cell-adhesion proteins designed for directed synaptogenesis: 1SZ-Nrxn1β (presynaptic): β-neurexin scaffold fused to a synthetic SynZip coiled-coil domain. 2SZ-Nlgn1 (postsynaptic): neuroligin-1 scaffold fused to the complementary SynZip domain. These proteins act as a programmable “molecular Velcro” that preferentially drives the formation of specific synapses between neurons expressing the matching pair, overcoming the random connectivity of native neurexin–neuroligin interactions. Why?https://pages.htgaa.org/2026b/david-morales/week-02-hw-dna-design/index.htmlMon, 01 Jan 0001 00:00:00 +0000https://pages.htgaa.org/2026b/david-morales/week-02-hw-dna-design/index.htmlPart 1: Defining the expression target Target molecule I'm expressing a pair of orthogonal adhesion proteins. For this project I'm using GFP and a anti-GFP binding protein described by Stevens et al. (Nature 2022). Each synCAM consists of: An extracellular interaction domain: one partner carries superfolder GFP (sfGFP) and the complementary partner carries the high-affinity anti-GFP nanobody LaG16. A transmembrane domain. An intracellular domain derived from ICAM-1, which links the adhesion complex to the cytoskeleton and determines the mechanical properties of the cell–cell interface. This pair enables heterophilic, orthogonal adhesion: cells expressing the GFP-version preferentially adhere only to cells expressing the LaG16-version, allowing directed multicellular assembly and, in the longer term, programmable synaptogenesis or tissue reorganization.https://pages.htgaa.org/2026b/david-morales/final-project/index.htmlMon, 01 Jan 0001 00:00:00 +0000https://pages.htgaa.org/2026b/david-morales/final-project/index.html