Study On Relationship Between Amino Acid Sequence And Function Of Membrane Active Peptide Melittin

Membrane active peptides(especially pore-forming peptides)have great potential value in many biomedical applications.However,the basic molecular mechanisms of these peptides are poorly understood,which seriously impedes the design and modification of membrane active peptides that is necessary for a specific purpose in practical applications.In the work of this paper,we take the pore forming peptide Melittin and function enhanced mutants as an example,the molecular dynamics simulation for this kind of polypeptide and lipid bilayer interaction process was studied and the pore forming behavior of peptides were depicted from two aspects of dynamics and thermodynamics,which gives some of the basic relationship between amino acid sequence and function.In particular,we found that the 10 position of the Melittin amino acid sequence determines the ability of the peptide chain to be elastomeric(e.g.,U-shaped),while residues near the C terminus affect the degree of aggregation between the peptides.The results of our study explain the complex interaction mechanism between membrane active peptide Melittin and lipid bilayer from the perspective of amino acid sequence-structure-function relationship and the possible pathways to enhance the function of polypeptides,which have important guiding significance for the optimization and design of membrane active peptides in the future.