Conformational Dynamics of Glucagon-like Peptide-2 with Different Electric Field

Molecular dynamics (MD) simulation was used to study the influence of electric field on Glucagon-like Peptide-2 (GLP-2). Different electric field strengths (0 V/nm <= E <= 1 V/nm) were mainly carried out on GLP-2. The structural changes in GLP-2 were analyzed by the Root Mean Square Deviation (RMSD), Root Mean Square Fluctuation (RMSF), Radius of Gyration (Rg), Solvent Accessible Surface Area (SASA), Secondary Structure and the number of hydrogen bonds. The stable alpha-helix structure of GLP-2 was unwound and transformed into an unstable Turn and Coil structure since the stability of the GLP-2 protein structure was reduced under the electric field. Our results show that the degree of unwinding of the GLP-2 structure was not linearly related to the electric field intensity. E = 0.5 V/nm was a special point where the degree of unwinding of the GLP-2 structure reached the maximum at this electric field strength. Under a weak electric field, E < 0.5 V/nm, the secondary structure of GLP-2 becomes loose, and the entropy of the chain increases. When E reaches a certain value (E > 0.5 V/nm), the electric force of the charged residues reaches equilibrium, along the z-direction. Considering the confinement of moving along another direction, the residue is less free. Thus, entropy decreases and enthalpy increases, which enhance the interaction of adjacent residues. It is of benefit to recover hydrogen bonds in the middle region of the protein. These investigations, about the effect of an electric field on the structure of GLP-2, can provide some theoretical basis for the biological function of GLP-2 in vivo.

Automated summary

Molecular dynamics simulation was used to explore the effect of electric field on the structure of Glucagon-like Peptide-2 (GLP-2). The stable α-helix structure of GLP-2 was unwound and transformed into an unstable Turn and Coil structure under the electric field. The degree of unwinding was not linearly related to the electric field intensity, with a maximum at E = 0.5 V/nm. Under weak electric fields, the secondary structure of GLP-2 became looser and chain entropy increased. At a certain electric field strength, the electric force of charged residues reached equilibrium, leading to reduced residue freedom, decreased entropy, increased enthalpy, and enhanced interaction between adjacent residues.