In 2008 and 2009, Professor Donghai Lin’s research team at SIMM（Shanghai Institute of Materia Medica） and Professor Ren Lai’s team at Kunming Institute of Zoology have worked together on molecular mechanisms and structural basises for several crucial peptides with significant biological functions.

　　They have made remarkable achievements represented by the following high-quality thesis: (1) they addressed the molecular mechanism and structural basis for a frog (odorrana livida) to fast eliminate free radical from its naked skin to keep redox homeostasis by an antioxidant peptide antioxidin-RL. This work established the theoretical foundation for the further development of antioxidin-RL in the biomedicine, anti-oxidation protection and cosmetics. Two articles have been published for this work: Mol. Cell Proteomics,2009,8 (3): 571-583, Free Radic Biol. Med.，2010, Feb 2. (2) They described the molecular mechanism for a neurotoxin called anntoxin (59 a.a) which was identified for the first time from an amphibian (tree frog) and might take effect through the potassium ion channel. This work interpreted the solution structure of the anntoxin and established a theoretical foundation for the further development of the neurotoxin. They have published this work in J. Biol. Chem., 2009，284 (33): 22079-22086, which was highlighted as a substantial finding by the American Society of Biochemistry and Molecular Biology. (3) They also established the structural basis for a natural antibacterial peptide called cathelicidin-BF which was the first gene-coded neurotoxin found in amphibians Potent, broad spectrum, salt-independent antimicrobial activities make cathelicidin-BF an excellent candidate for clinical or agricultural antibiotics. This work provided important structural information for the further research on cathelicidin-BF and also for the development of potential peptide antibiotics. This paper has been published in PLoS ONE, 2008，3 (9): e3217 and was selected by Nature China as a highlighting paper. (4) They determined the solution structure of a lectin peptide called odorranalectin (with the smallest molecular weight in the world), elucidated the molecular mechanism of odorranalectin binding with the L-fucose. This work has been published in PLoS ONE，2008，3 (6): e2381. Dorrananlectin showed extremely low toxity and immunogenicity in mice. Moreover, this peptide adopts a very stable ternary structure and can specifically bind the L-fucose in the liver and the lung. Therefore it may be potentially developed to be a promising candidate for drug targets.

　　(Source of News: Research Team of Professor Donghai Lin)