Dr Teh Aik Hong studies protein functions and structures by using X-ray crystallography, computational docking and molecular dynamics. He is currently working on polysaccharide-degrading enzymes such as alginate lyase, which cleaves the negatively charged sugar alginate into unsaturated oligosaccharides that possess biological activity. Preliminary collaborative studies from his lab have shown that the degraded alginate extended the lifespan of worms and improved the rough-eye phenotype of fruit flies with Alzheimer’s disease. Other ongoing collaborations include the use of the enzyme in drug delivery and testing of the unsaturated alginate on cancer cells.

Aik Hong is also employing in silico techniques in addition to empirical methods to study how the giant mTOR complexes, which are the master regulators of cell growth and ageing conserved from yeast to humans, are regulated by DEPTOR which inhibits mTOR. He has previously worked on PhaC too, an enzyme which produces polyhydroxyalkanoate (PHA) bioplastics that have huge potential to replace petroleum-based plastics. Using a novel docking protocol that he developed, his analysis has provided new insights into PHA polymer elongation and substrate specificity, knowledge that can be used to improve the enzyme's activity. Other proteins that he has studied include Salmonella toxin–antitoxin systems, bacterial haemoglobins, phosphatase and cytidine deaminase. After gaining valuable experience in protein structures, he is now embarking on engineering enzymes with new activity and designing peptides as drugs.

Aik Hong obtained his BSc and MSc from Tokyo Institute of Technology under the Monbukagakusho scholarship from the Japanese government, and continued with DSc under a scholarship from the Tokio Marine Kagami Memorial Foundation. He worked as a postdoctoral researcher at SPring-8 in 2007, one of the largest synchrotron radiation facilities in the world, and came back to his hometown in 2009 to join CCB as a postdoctoral fellow. He became a contract lecturer in 2013.