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Revision as of 17:29, 12 November 2006
MIT Fall 2006
- 5.07 Biological Chemistry I
- 7.03 Genetics
- 20.310 Molecular, Cellular and Tissue Biomechanics
- 20.309 Biological Engineering II: Instrumentation and Measurement
- 20.181 Computation for Biological Engineers
- iMath Program
- Imperial iGEM 2006 - Biological Oscillator based upon Predator-Prey interactions using quorum sensing molecules.
- 2004 - present: Imperial College, London - BEng in Biomedical Engineering with a year abroad at MIT, 3rd Year
- Summer 2005: Harvard Summer School, Organic Chemistry (S-20ab)
- 2002 - 2004: British School in the Netherlands (Voorschoten, Netherlands)
- 2000 - 2002: St. John's School (Houston, TX, USA)
- Sport – Swimming and Badminton
- Travel – Travel over Europe, Asia, Africa, and North America
- Arts – frequent concerts, plays, and musicals as well as enjoy visiting art galleries and reading classics
More Random Stuff About Me
- Favourite Colours: Orange & Blue
- Ethnic Origin: Chinese from the Philippines
- Place I would like to retire: somewhere in the USA
- Quote I like: "God grant me the serenity to accept the things I cannot change, to change the things I can, and the wisdom to know the difference"
- Religious Affiliation: None
- What I wanted to be when I grew up: pilot, businessman, lawyer, among other things
- What I want to do now: medicine
- Places I haven't been that I want to go: Australia & New Zealand
- My best place to relax: a remote island in the Philippines
- One thing I can't live without: internet...:)
20.310 Term Paper
Analysis of Human Immunodeficiency Virus Type I gp120 Receptor Interactions and its Implications on Future HIV Drug Therapy. (A single paper critique)
In Single-Molecule Analysis of Human Immunodeficiency Virus Type 1 gp120-Receptor Interactions in Living Cells, the authors give a quantitative description of the binding forces and dissociation constants of the gp120/cd4/CCR5 receptor complex using a molecular force probe. Experimental data is fitted to the Bell model relating the rupture force required to break a bond between two molecules to the applied loading rate. The breakthrough proposed in this paper is providing a quantitative analysis of the forces involved in viral-host cell interactions which may lead to a better understanding of the mechanisms of viral infection. Once we successfully elucidate the molecular mechanism of viral entry, we can then propose innovate drug treatments capitalizing on HIV-1 entry inhibition.
The experimental method used by Chang, et al., is similar to the use of atomic force microscopy experiments we learnt in class to determine forces. They use a cantilever with the gp120 receptors attached and use it to probe the cell surface membrane containing only the CD4 host receptors, only the CCR5 chemokine receptors, or a combination of both receptors.
Although experimentally it was shown that the force required to break the gp120/CD4/CCR5 bond was similar to that required to break the bond between gp120 and CD4, the bond between formed between all three coreceptors lasted significantly longer than the gp120-CD4 bond.
Studies have been shown that persons with a delta32 mutation coding for the CCR5 have a much lower HIV infection rate than individuals that are wild type. Thus, understanding the mechanics behind the CCR5 interaction with the gp120 receptor protein could help in elucidating why such individuals with mutations have a much lower prevalence of HIV. This could be significant in leading to therapies aimed at modulating the receptor binding, potentially affecting the lives of millions of AIDS sufferers.
- Chang MI, Panorchan P, Dobrowsky TM, Tseng Y, and Wirtz D. . pmid:16282475.
- Doranz BJ, Baik SS, and Doms RW. . pmid:10559353.
- Hill CM, Deng H, Unutmaz D, Kewalramani VN, Bastiani L, Gorny MK, Zolla-Pazner S, and Littman DR. . pmid:9261346.
- Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, and Hendrickson WA. . pmid:9641677.
- Wu L, Gerard NP, Wyatt R, Choe H, Parolin C, Ruffing N, Borsetti A, Cardoso AA, Desjardin E, Newman W, Gerard C, and Sodroski J. . pmid:8906795.