Programme Book - UPM - Universiti Putra Malaysia

P38 DESIGN, SYNTHESIS AND ACTIVITY STUDIES OFNOVEL ANTIFREEZE PEPTIDE DERIVED FROM SHORTHORNSCULPIN ANTIFREEZE PROTEINA.A. Suratman, N. Abu Bakar, B. A. Tejo*Department of Chemistry, Faculty of Science, Universiti Putra Malaysia, 43400 UPMSerdang, Selangor, MalaysiaCorresponding author: bimo@upm.edu.myOrganisms that live in cold environment are able to survive due to their uniquecharacteristic, in which they are able to produce antifreeze proteins (AFPs). AFPswork by inhibiting the ice crystal growth and suppressing the water freezing point,which eventually could harm the organisms. The unique functions of AFPs haveattracted interests in utilizing the proteins for industrial or medical applications. In thisstudy, we aimed to design novel antifreeze peptides derived from the structure ofshorthorn sculpin antifreeze protein. It has been suggested that the helical segment ofsequence of shorthorn sculpin AFP is responsible for the antifreeze activity. Threepeptides derived from the sequence of shorthorn sculpin AFP had been designed andsynthesized using solid phase peptide synthesis with Fmoc-protected amino acids onRink amide resin. The antifreeze activity of the synthesized peptides was measured byice recrystallization inhibition (IRI) assay. The structure of antifreeze peptides wasdetermined using Fourier Transform Infrared Spectroscopy (FTIR). Our resultsshowed that the helical structure and the extent of peptide helicity play very importantrole in enhancing the antifreeze activity of the peptides derived from shorthornsculpin AFP sequence.53 |16 th Industrial Chemistry Seminar: Chemistry- A Passport to a Brighter Future