Peptide | PEF^{a} | PPSA^{b} | MPCA^{c} | ln P^{d} | PSA^{e} |
---|---|---|---|---|---|

Ser^{1}-PMP-1 | −0.23 | 5,142 ± 62 | 0.006 | −15.76 | 2,600 |

Asp^{1}-PMP-1 | −0.21 | 5,142 ± 151 | 0.007 | −18.28 | 2,900 |

hPF-4 | −0.22 | 4,034 ± 67 | 0.007 | −15.76 | 2,100 |

↵

*a*PEF, positional energy function (in kiloteslas). Mean residue energies are indicated for peptides in their monomeric forms. See Materials and Methods.↵

*b*PPSA, partial positive surface area (in angstroms squared) (25). Peptide (monomeric form) motion was simulated by molecular dynamics at 310 K. The mean partial positive surface area ± standard deviation was computed for the resulting ensemble of peptide conformers. The partial positive surface area is a measure of the amount of peptide surface that carries a net positive charge. Since the side chains of the peptides are in motion at realistic temperatures, the use of molecular dynamics provides a realistic estimate of the properties of the peptides.↵

*c*MPCA, most positive charged atom, defined as the charge on the most positively charged atom divided by the sum of all positive charges. The quantity is a unitless ratio.↵

*d*ln P, logarithm of the partition coefficient based on Hansch relationships. The HINT program was used to estimate this parameter by the dictionary method (31).↵

*e*PSA, polar surface area (in angstroms squared).