Experimental proofs of the leucine properties due to steric effect and hydrophobic interactions: leucine prevent aggregation and is a good helical promoter. The leucine in first position imposes a change of backbone direction to the following residues. We have further proved this property studying a multifunctional LVV-hemorphin. The initial basic NMR data analysis of synthetic homologous Boc-L1-V2-V3-Y4-P5-OMe clearly indicates the coexistence of three different conformations in equilibrium. NMR data and molecular dynamic calculation point to a ?-turn conformation stabilized by an hydrogen bond, i.e (Y4)NH----O=C(V2), for the main conformation (85%).This might mean that steric and hydrophobic interactions stabilizes further the trans conformation of penta-peptide. Such stabilization can be quantified looking to trans/cis difference (20%) between Boc-Y1-P2-OMe and Boc-L1-V2-V3-Y4-P5-OMe.
Conformational changes and other biophysical properties of leucine-containing peptides
Fenude Emma
2019
Abstract
Experimental proofs of the leucine properties due to steric effect and hydrophobic interactions: leucine prevent aggregation and is a good helical promoter. The leucine in first position imposes a change of backbone direction to the following residues. We have further proved this property studying a multifunctional LVV-hemorphin. The initial basic NMR data analysis of synthetic homologous Boc-L1-V2-V3-Y4-P5-OMe clearly indicates the coexistence of three different conformations in equilibrium. NMR data and molecular dynamic calculation point to a ?-turn conformation stabilized by an hydrogen bond, i.e (Y4)NH----O=C(V2), for the main conformation (85%).This might mean that steric and hydrophobic interactions stabilizes further the trans conformation of penta-peptide. Such stabilization can be quantified looking to trans/cis difference (20%) between Boc-Y1-P2-OMe and Boc-L1-V2-V3-Y4-P5-OMe.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
