The present invention provides an evaluating system and the use thereof for the efficacy of antimicrobial peptide, which includes the following steps: (a) constructing a peptide by a first input unit, and load the peptide into an aqueous solution for a first time for equilibration; (b) constructing a lipid bilayer by a second input unit, and load the lipid bilayer into an aqueous solution for a second time for equilibration; (c) Using a first processing unit, simulations are carried out for an aqueous system containing an equilibrated peptide from the first input unit and the equilibrated lipid bilayer from the second input unit; (d) calculating the partition free energy of the peptide by a second processing unit; (e) outputting the prediction by an output unit, wherein the output unit is connected with the first processing unit and the second processing unit.
Please help me write a proper abstract based on the patent claims. CLAIM: 1. An evaluating system for the efficacy of antimicrobial peptides, includes: (a) a first input unit, wherein the first input unit is for constructing a peptide; (b) a second input unit, wherein the second input unit is for constructing a lipid bilayer; (c) a first processing unit, which is connecting with the first input unit and the second input unit, the first processing unit is conducting a molecular dynamics (MD) simulations in an aqueous solution with peptides constructed by the first input unit and the lipid bilayer constructed by the second input unit; (d) a second processing unit, connected with the first processing unit, is to calculate <Ni> that is the moving average of the number of heavy atoms in the antimicrobial peptide contacting hydrophobic lipid tails and <No> that is the moving average of the numbers of heavy atoms in the antimicrobial peptide not contacting hydrophobic lipid tails during a 4 ns window; and a partition free energy (ΔGp) is calculated based on <Ni> and <No>; wherein the heavy atoms are all the non-hydrogen atoms; and (e) predicted partition free energy (ΔGp) and/or predited peptide activity are outputted by an output unit, wherein the output unit is connected with the second processing unit; wherein the first input unit, the second input unit, the first processing unit, the second processing unit and the output unit are operated by a computer. 2. The evaluating system of claim 1, wherein the first input unit includes a peptide that is designed by a software including PyMol or Discovery Studio Visualizer, or determined by experiments including X-ray crystallography or NMR; wherein the peptide is equilibrated in simulations conducted by simulation software including NAMD, VMD, AMBER, GROMACS with commonly used force field including CHARMM, AMBER, GROMOS and OPLS under physiological conditions. 3. The evaluating system of claim 1, wherein the second input unit includes an “CHARMM-GUI” server to build the lipid bilayer; wherein the lipid bilayer is equilibrated in simulations conducted by simulation software including NAMD, VMD, AMBER, GROMACS with commonly used force field including CHARMM, AMBER, GROMOS and OPLS under physiological conditions. 4. The evaluating system of claim 1, wherein the first processing unit that utilizes simulation software including NAMD, VMD, AMBER, GROMACS with commonly used force field including CHARMM, AMBER, GROMOS and OPLS to equilibrate inserted peptides in the lipid bilayer. 5. The evaluating system of claim 1, wherein the lipid bilayer comprising palmitoyloleoyl phosphatidyl choline (POPC) and/or palmitoyloleoyl-phosphatidylglycerol (POPG). 6. The evaluating system of claim 1, wherein the molecular dynamics (MD) simulation system that is to first make the hydrophobic side of the antimicrobial peptide face the pre-equilibrated lipid bilayer; then a sink and surface simulation is carried out after the projections of mass centers of the peptide and lipid bilayer on the normal of lipid bilayer being positioned 35 Å apart from each other. 7. The evaluating system of claim 6, wherein the sink and surface simulate ion that is to pull the helical peptide by a weak force to where a few Ångstrom below the average coordinate of the phosphor atoms in the upper leaflet of the lipid bilayer and to hold the peptide therein for several nanoseconds; afterwards, the weak restraint is released, and within 10 to 35 nanoseconds the helical peptide can float (surface) onto the membrane surface and equilibrate therein. 8. A prediction method for antimicrobial efficacy of antimicrobial peptides based on the evaluating system of claim 1, which comprises the following steps: (a) a first input unit, wherein the first input unit is for constructing a peptide; (b) a second input unit, wherein the second input unit is for constructing a lipid bilayer; (c) a first processing unit, which is connecting with the first input unit and the second input unit, the first processing unit is conducting a molecular dynamics (MD) simulations in an aqueous solution with peptides constructed by the first input unit and the lipid bilayer constructed by the second input unit; (d) a second processing unit, connected with the first processing unit, is to calculate <Ni> that is the moving average of the number of heavy atoms in the antimicrobial peptide contacting hydrophobic lipid tails and <No> that is the moving average of the numbers of heavy atoms in the antimicrobial peptide not contacting hydrophobic lipid tails during a 4 ns window; and partition free energy (ΔGp) is calculated based on <Ni> and <No>; wherein the heavy atoms are all thenon-hydrogen atoms; and (e) predicted partition free energy (ΔGp) and/or predited peptide activity are outputted by an output unit, wherein the output unit is connected with the second processing unit. 9. The method of claim 8, wherein features a simulation where antimicrobial peptide is equilibrated in a solution for a few hundred picoseconds. 10. The method of claim 8, wherein the first input unit includes a peptide that is designed by a software including PyMol or Discovery Studio Visualizer, or determined by experiments including X-ray crystallography or NMR; wherein the peptide equilibration is conducted by simulation software including NAMD, VMD, AMBER, GROMACS with commonly used force field including CHARMM, AMBER, GROMOS and OPLS under physiological conditions. 11. (canceled) 12. (canceled) 13. (canceled) 14. The prediction method of claim 8, further comprises predicting antimicrobial activity of the antimicrobial peptide. 15. The prediction method of claim 8, wherein the molecular dynamics (MD) simulation system that is to first make the hydrophobic side of the antimicrobial peptide face the pre-equilibrated lipid bilayer, and a sink and surface simulation is then carried out after the projections of mass centers of the peptide and lipid bilayer on the normal of lipid bilayer being positioned 35 Å apart from each other. 16. The prediction method of claim 8, wherein the sink and surface simulate ion that is to pull the helical peptide by a weak force to where a few Ångstrom below the average coordinate of the phosphor atoms in the upper leaflet of the lipid bilayer and to hold the peptide therein for several nanoseconds; afterwards, the weak restraint is released, and within 10 to 35 nanoseconds the helical peptide can float onto the membrane surface and equilibrate therein. 17. The prediction method of claim 8, further comprising using partition free energy calculation of the quantity ΔGp=−kBTln(<Ni>/<No>) or =−kBT(<lnNi>/<lnNo>), where kB is the Boltzmann constant, T is the absolute temperature, Ni is the average number of heavy atoms of antimicrobial peptide contacting hydrophobic lipid tails and the No is the average number of heavy atoms of antimicrobial peptide that do not contact hydrophobic lipid tails; the < > symbol denotes moving averages of a 4 nanosecond window. 18. An antimicrobial peptide with low hemolytic activities can be expressed by the following formula: xAP1yBP2zCn(P3vD) (formula I); wherein the x, y, z, v and n are all positive integers; and x=0˜6, y=0 or 4, z=0˜6, v=0˜4 and n=0 or 1 each of P1, P2 and P3 is -Trp-Leu-Lys-; A, B and C are selected from the group of Trp, Leu and Lys and D is Lys. 19. The antimicrobial peptide of claim 18, wherein the antimicrobial peptides are selected from a group of SEQ ID NO:2 to SEQ ID NO:13.