Associate Professor LAM Yulin

B.Sc.(Hons), National University of Singapore, 1987; Ph.D., National University of Singapore, 1992; Research Fellow, The Scripps Research Institute, 1992-1994; Research Fellow, Institute of Molecular and Cell Biology, 1994-1996.

Contact Information 

Office: S5-03-04
Tel: (65)-6516-2688 | Fax: (65)-6779-1691


ORCID: 0000-0003-0984-9492
ResearcherID: B-1755-2018


Research Interests

Our research interests include (i) bioorganic and medicinal chemistry, and (ii) green chemical synthesis. Specific foci are:

  • Synthesis and biological evaluations of novel organic compounds and natural product derivatives as potential anti-cancer, anti-inflammatory and neurological agents;
  • Development of recyclable, fluorous reagents and catalysts for organic transformations in water.


Research Highlight

Ref: Chern, J.; Lu, C.-P.; Fang, Z.; Chang, C.-M.; Hua, K.-F.; Chen, Y.-T.; Ng, C. Y.; Chen, Y.-L. S.; Lam, Y.; Wu, S.-H., "Affinity-driven Covalent Modulator of Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) Cascade" Angew. Chem. Int. Ed. 2018, 10.1002/anie.201801618

Overcoming resistance: A new class of inhibitors that target the noncatalytic C247 residue of GAPDH in an affinity‐driven manner to initiate SIAH1‐dependent apoptosis and androgen‐receptor degradation has been discovered. The affinity‐driven Michael addition of isochaihulactone was found to control the “ON/OFF” switch of apoptosis by a mechanism that bypasses the common apoptosis‐resistant route of multiple‐drug‐resistant cancers.



Figure shows the targeting of cPLA2 by the newly-designed inhibitor and substrate probes. Left: Identifying differences in cPLA2 level in untreated and Trichostatin A (TSA)-treated SHSY5Y cells. Right: FRET-based assay with the use of substrate probe that demonstrates higher selectivity for cPLA2 against sPLA2.

Ref: Ng, C. Y.; Kwok, T. X. W.; Tan, F. C. K.; Low, C.-M.; Lam, Y. Fluorogenic Probes to Monitor Cytosolic Phospholipase A2 Activity. Chem. Commun. 2017, 53, 1813.

Cytosolic phospholipase A2 (cPLA2) is an ubiquitous enzyme which is highly selective for glycerol-phospholipids containing arachidonic acid (AA). There has been much interest to understand the molecular mechanism regulating this enzyme and to develop therapeutics for the treatment of cPLA2-upregulated diseases. Herein we have developed AA derivatives equipped with either one or two fluorescent groups which function as inhibitor and substrate probes of cPLA2. The inhibition was shown to perform dual functions of inhibition and imaging while the substrate probe could be used for activity assay.


Teaching Contributions

  • CM1121 Organic Chemistry 1


Representative Publications