Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/54768
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dc.contributor.authorGiam, Zhen Gan.
dc.date.accessioned2013-08-13T01:16:34Z
dc.date.available2013-08-13T01:16:34Z
dc.date.copyright2013en_US
dc.date.issued2013
dc.identifier.urihttp://hdl.handle.net/10356/54768
dc.description.abstractResearches on Antimicrobial Peptides (AMPs) are fumed by the rise of multidrug resistant (MDR) bacteria. Multiple physiochemical properties are identified to have contributions to antimicrobial activities of these peptides. Based on the information, 5 peptides were designed with the following parameters: helical, short in sequences, contain arginine and tryptophan residues, cationic and high in hydrophobic content that led to amphipathic. Their biological activities and peptides–lipids interactions were investigated. Ultimately, the peptide with the highest positive charge, lowest hydrophobicity and without tryptophan showed greatest potency against the tested bacteria. While 3 other peptides mainly showed comparable, but slightly lowered antimicrobial activities. Cationicity and hydrophobicity are important for initial peptides–membranes bindings, but increasing of these factors was not shown to increase their initial binding or antimicrobial effects. Specific amino acids like Arg and Trp might not be necessary for bindings and activities, in the case of potential helical peptides. Also, AMPs’ higher ability to bind to the membrane might not equate to better ability to kill bacteria.en_US
dc.format.extent30 p.en_US
dc.language.isoenen_US
dc.rightsNanyang Technological University
dc.subjectDRNTU::Scienceen_US
dc.titleDesigned Trp/Arg-rich antimicrobial peptides.en_US
dc.typeFinal Year Project (FYP)en_US
dc.contributor.supervisorSurajit Bhattacharyyaen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.degreeBachelor of Science in Biomedical Sciencesen_US
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Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)
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