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#Chang1 pmid=16282475
#Chang1 pmid=16282475
#Doms00 pmid=11069884
#Doranz99 pmid=10559353
#Doranz99 pmid=10559353
#Hill97 pmid=9261346
#Hill97 pmid=9261346

Revision as of 23:40, 17 November 2006

John Sy

Contact Information:

E-mail: (at), syjohn (at), syjohn (at)

MIT Spring 2007 (Tentative)

  • 7.02 Biology Lab or 20.109 Biological Engineering Lab
  • 7.06 Cell Biology
  • 20.330 Fields, Forces, and Flows in Biological Systems
  • 20.390 Foundations of Computational and Systems Biology

MIT Fall 2006

Imperial iGEM



  • 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

  1. Favourite Colours: Orange & Blue
  2. Ethnic Origin: Chinese from the Philippines
  3. Place I would like to retire: somewhere in the USA
  4. 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"
  5. Religious Affiliation: None
  6. What I wanted to be when I grew up: pilot, businessman, lawyer, among other things
  7. What I want to do now: medicine
  8. Places I haven't been that I want to go: Australia & New Zealand
  9. My best place to relax: a remote island in the Philippines
  10. 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.

Prelimiarly Bibliography

  1. Chang MI, Panorchan P, Dobrowsky TM, Tseng Y, and Wirtz D. . pmid:16282475. PubMed HubMed [Chang1]
  2. Doms RW and Trono D. . pmid:11069884. PubMed HubMed [Doms00]
  3. Doranz BJ, Baik SS, and Doms RW. . pmid:10559353. PubMed HubMed [Doranz99]
  4. Hill CM, Deng H, Unutmaz D, Kewalramani VN, Bastiani L, Gorny MK, Zolla-Pazner S, and Littman DR. . pmid:9261346. PubMed HubMed [Hill97]
  5. Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, and Hendrickson WA. . pmid:9641677. PubMed HubMed [Kwong98]
  6. 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. PubMed HubMed [Wu96]
  7. Urnov FD, Miller JC, Lee YL, Beausejour CM, Rock JM, Augustus S, Jamieson AC, Porteus MH, Gregory PD, and Holmes MC. . pmid:15806097. PubMed HubMed [Urnov00]
All Medline abstracts: PubMed HubMed
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