Nuclear Magnetic Resonance Study of the Peptide FRANCESSEPAROVIC

JA Karas; DW Keizer; MA Sani

Journal article

Nuclear Magnetic Resonance Study of the Peptide FRANCESSEPAROVIC

JA Karas, DW Keizer, MA Sani

Australian Journal of Chemistry | CSIRO PUBLISHING | Published : 2020

DOI: 10.1071/CH19357

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Abstract

As an eminent ambassador of STEM and renowned NMR spectroscopist, Frances Separovic is an internationally famous name, but could it also be a valuable membrane-active peptide sequence? Her name has been used as an amino acid sequence (FS), successfully synthesised, oxidised, and put into contact with membrane models to investigate any serendipitous activity. The 3D structure of the cyclic FS was determined in dodecylphosphocholine (DPC) micelles by solution NMR spectroscopy. FS displayed a twisted bend separating a helical stretch and an unstructured segment. Using solid-state NMR spectroscopy, the effect of FS on 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dimyristoyl-sn-glyc..

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University of Melbourne Researchers

John Karas Author

David Keizer Author

Marco Sani Author

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Grants

Awarded by Australian Research Council

Funding Acknowledgements

This research was funded by the Australian Research Council (ARC) Discovery Project grant DP160100959 to F.S. and LIEF grant LE160100120 to F.S., D.K. Keizer, and M.-A.S. Access to the NMR spectrometers was supported through a collaboration with the Bio21 Institute, Melbourne University, Australia. The authors are grateful for having had the opportunity to work with Professor Separovic and would like to convey to her their best wishes for her future endeavours.