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Biology subjects

Sutton, M. J.

Publications and source records attributed to Sutton, M. J..

2 recordsLinked to original sources

LC-MS analysis of RNA through hydrogen bonding of alkylamines

Nucleic acid oligonucleotides represent a promising therapy for treating disease. Production of these biopolymers happens synthetically which can produce impurities concomitant with the desired product. The use of liquid chromatography coupled to high resolution mass spectrometry is a robust analytical technique for determination of sample purity. Traditionally, ion pairing reagents are used to facilitate chromatography separation before sampling with the mass spectrometer. The choice of reagent for analysis can impact the analysis as the length of the oligonucleotide increases. This is in part due to the thermodynamics of transitioning the oligonucleotide from the liquid phase to the gas phase. Here we show that the use of a hydrogen bond donating alkylamine assists with overcoming the energy barrier of phase transition by bonding to the nucleobase as well as the phosphodiester backbone. By increasing the relative hydrophobicity of the oligonucleotide, the transition to the gas phase is increased producing a cleaner mass spectrum. Furthermore, we show that by using a hydrogen bond donating alkylamine, we can remove the fluoroalcohol reagent commonly used in ion pairing mass spectrometry of nucleic acids.

biochemistry↗

Parallel evolution of frog antimicrobial peptides produces identical conformations but subtly distinct membrane and antibacterial activities

Frogs such as Rana temporaria and Litoria aurea secrete numerous closely related antimicrobial peptides (AMPs) as an effective chemical dermal defence. Despite the high similarity in physical properties and preference for adopting secondary amphipathic, -helix conformations in membrane mimicking milieu, their spectrum of activity and potency often varies considerably. Damage or penetration of the bacterial plasma membrane is considered essential for AMP activity and hence distinguishing apparently similar AMPs according to their behaviour in, and effects on, model membranes will inform understanding of species specific effective antimicrobial mechanisms. Here we use a combination of molecular dynamics simulations, circular dichroism and patch-clamp to investigate the basis for differing anti-bacterial activities in representative AMPs from each species; temporin L and aurein 2.5. Despite adopting near identical, -helix conformations in the steady-state in a variety of membrane models, these two AMPs can be distinguished both in vitro and in silico based on their dynamic interactions with model membranes; the greater conformational flexibility and the higher amplitude channel conductance induced offers a rationale for the greater potency and broader spectrum of activity of temporin L over aurein 2.5. Specific contributions from individual residues are identified that define the mechanisms of action of each AMP. Our findings suggest AMPs in frogs are examples of parallel evolution whose utility is based on apparently similar but subtly distinct mechanisms of action.

biophysics↗