Skip to main content
. 2004 Apr 26;101(19):7363–7368. doi: 10.1073/pnas.0401567101

Table 1. Quantification of 3D congruence among disulfide-containing antimicrobial peptides.

Peptide Length, aa rmsd, Å Identity, % Align/gap
Antimicrobial
Ah-AMP-1 (Aesculus, tree, 1BK8) 50 0.0 100 50/0
Sapecin (Sarcophaga, fly, 1L4V) 40 0.9 25.0 38/0
Protegrin-1 (Sus, Pig, 1PG1) 19 1.2 18.8 16/0
Defensin (Raphanus, radish, 1AYJ) 51 1.3 47.6 49/0
Drosomycin (Drosophila, fruit fly, 1MYN) 44 1.4 29.3 41/6
Thionin (Triticalis, wheat, 1GPS) 47 1.8 26.1 46/3
MGD-1 (Mytilus, mussel, 1FJN) 39 2.0 26.5 34/1
Thanatin (Podisus, soldier bug, 8TFV) 21 2.2 12.5 16/0
HNP-3 (Homo, human, 1DFN) 34 3.2 8.3 24/17
MBD-8 (Mus, mouse, 1E4R) 35 3.4 0.0 24/13
AFP-1 (Aspergillus, fungus, 1AFP) 51 4.8 6.2 32/7
Mean ± SD 2.2 ± 1.2*
Model-predicted antimicrobial
Brazzein (Pentadiplandra, j'oublie berry, 1BRZ) 54 1.9 34.4 32/4
Charybdotoxin (Leiurus, scorpion, 2CRD) 37 2.0 17.4 46/2
Mean ± SD 1.9 ± 0.7*
Nonantimicrobial
Transforming growth factor α (Homo, human, 3TGF) 50 4.7 3.1 32/7
Metallothionein (Saccharomyces, yeast, 1AOO) 40 5.3 18.8 32/16
Allergen-5 (Ambrosia, ragweed, 2BBG) 40 6.5 18.8 32/7
Ferredoxin (Clostridium, Bacterium, 2FDN) 55 7.4 5.0 40/6
Mean ± SD 6.0 ± 1.2

Conformation alignments of antimicrobial and nonantimicrobial peptide structures were analyzed by pairwise comparison with Ah-AMP-1 (Aesculus, horse chestnut tree, 1BK8) by using combinatorial extension. Peptide formatting: peptide (source genus, common name, PDB ID code). Control peptides (Fig. 2 I-L) were equivalent to Ah-AMP-1 in disulfide content, sequence length, and mass. Representative data are shown. All rmsd values were determined for distances between α-carbon atoms over the length of the alignment. Identity is percentage sequence identity between comparators. Align/gap indicates the number of residues aligned, and number of gaps inserted. *, rmsd values significantly different from nonantimicrobial peptides (two-tailed t test; P < 0.01).