Associating Biological Activity and Predicted Structure of Antimicrobial Peptides from Amphibians and Insects

dc.contributor.authorRichter, Amelia
dc.contributor.authorSutherland, Darcy
dc.contributor.authorEbrahimikondori, Hossein
dc.contributor.authorBabcock, Alana
dc.contributor.authorLouie, Nathan
dc.contributor.authorLi, Chenkai
dc.contributor.authorCoombe, Lauren
dc.contributor.authorLin, Diana
dc.contributor.authorWarren, René L.
dc.contributor.authorYanai, Anat
dc.contributor.authorKotkoff, Monica
dc.contributor.authorHelbing, Caren C.
dc.contributor.authorHof, Fraser
dc.contributor.authorHoang, Linda M.N.
dc.contributor.authorBirol, Inanc
dc.descriptionOpinions expressed in this document are those of the author and not necessarily those of the Governments of Canada and British Columbia. The Governments of Canada and British Columbia and their directors, agents, employees, or contractors will not be liable for any claims, damages, or losses of any kind whatsoever arising out of the use of, or reliance upon, this information.en_US
dc.description.abstractAntimicrobial peptides (AMPs) are a diverse class of short, often cationic biological molecules that present promising opportunities in the development of new therapeutics to combat antimicrobial resistance. Newly developed in silico methods offer the ability to rapidly discover numerous novel AMPs with a variety of physiochemical properties. Herein, using the rAMPage AMP discovery pipeline, we bioinformatically identified 51 AMP candidates from amphibia and insect RNA-seq data and present their in-depth characterization. The studied AMPs demonstrate activity against a panel of bacterial pathogens and have undetected or low toxicity to red blood cells and human cultured cells. Amino acid sequence analysis revealed that 30 of these bioactive peptides belong to either the Brevinin-1, Brevinin-2, Nigrocin-2, or Apidaecin AMP families. Prediction of three-dimensional structures using ColabFold indicated an association between peptides predicted to adopt a helical structure and broad-spectrum antibacterial activity against the Gram-negative and Gram-positive species tested in our panel. These findings highlight the utility of associating the diverse sequences of novel AMPs with their estimated peptide structures in categorizing AMPs and predicting their antimicrobial activity.en_US
dc.description.sponsorshipThis research was funded by Genome Canada and Genome BC as part of the PeptAid (291PEP) project. Additional support was received through the Undergraduate Student Research Awards program of the Natural Sciences and Engineering Research Council of Canada. Funds were also received from the Office of the Vice-President, Research and Innovation of the University of British Columbia.en_US
dc.identifier.citationRichter, A., Sutherland, D., Ebrahimikondori, H., Babcock, A., Louie, N., Li, C., Coombe, L., Lin, D., Rm, W., Yanai, A., Kotkoff, M., Helbing, C. C., Hof, F., Hoang, L., & Birol, İ. (2022). Associating Biological Activity and Predicted Structure of Antimicrobial Peptides from Amphibians and Insects. Antibiotics, 11(12), 1710.
dc.subjectantimicrobial peptideen_US
dc.subjectAMP discoveryen_US
dc.subjectstructure predictionen_US
dc.subjectantimicrobial resistanceen_US
dc.titleAssociating Biological Activity and Predicted Structure of Antimicrobial Peptides from Amphibians and Insectsen_US


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