Journal:

Article Title: RL-37, an Alpha-Helical Antimicrobial Peptide of the Rhesus Monkey

doi: 10.1128/AAC.45.10.2695-2702.2001

Figure Lengend Snippet: Comparison of rhesus and human cathelicidin peptides. Both signal peptides (underlined) have 30 residues, of which 28 (93.3%) are identical. Both cathelin domains have 101 residues, of which 93 (92%) are identical. The mature domains (dotted underlined) of RL-37 and LL-37 both contain 37 residues, of which 25 (67.6%) are identical. Mature rhesus RL-37 has a mass of 4,100.9 Da, a theoretical pI of 11.20, and a net charge of +8. Mature human LL-37 has a mass of 4527.34, a pI of 10.61, and a net charge of +6. A vertical line connects identical residues, and a plus sign identifies conservative substitutions. Residues that differ in the human and rhesus peptides are shown in boldface type.

Article Snippet: This difference disappeared when the peptides were studied under low-salt conditions (no added NaCl) and was magnified when the NaCl concentration of the underlay gel was raised to 175 mM (Table ). table ft1 table-wrap mode="anchored" t5 TABLE 2 caption a7 Peptide Mean MEC (μg/ml) ± SEM a S. aureus 930918-3 S. aureus 710A MRSA ATCC 33591 S. epidermidis ATCC 49741 0 mM NaCl LL-37 1.39 ± 0.31 1.25 ± 0.11 1.72 ± 0.33 1.77 ± 0.28 mRL-37 0.98 ± 0.08 1.00 ± 0.10 1.33 ± 0.02 1.39 ± 0.12 LL-37 pentamide 2.42 ± 0.09 2.30 ± 0.27 2.52 ± 0.17 1.88 ± 0.22 100 mM NaCl LL-37 48.2 ± 10.6 16.1 ± 0.29 186 ± 16.7 23.6 ± 1.22 mRL-37 2.81 ± 0.11 ∗ 2.48 ± 0.04 ∗∗ ∗ 4.17 ± 0.30 ∗∗ ∗ 2.40 ± 0.09 ∗∗ ∗ LL-37 pentamide 3.47 ± 0.84 ∗ 2.75 ± 0.20 ∗∗ ∗ 3.41 ± 0.40 ∗∗ ∗ 2.14 ± 0.10 ∗∗ ∗ 175 mM NaCl LL-37 >250 193 ± 57.0 >250 110 ± 42.2 mRL-37 6.49 ± 0.30 ∗∗ ∗ 5.76 ± 0.27 ∗∗ ∗ 11.6 ± 0.90 ∗∗ ∗ 6.92 ± 0.38 ∗∗ ∗ LL-37 pentamide 4.63 ± 0.47 ∗∗ ∗ 4.82 ± 1.03 ∗∗ ∗ 4.69 ± 1.32 ∗∗ ∗ 4.31 ± 0.75 ∗∗ ∗ Open in a separate window a n = 3.

Techniques:

Journal:

Article Title: RL-37, an Alpha-Helical Antimicrobial Peptide of the Rhesus Monkey

doi: 10.1128/AAC.45.10.2695-2702.2001

Figure Lengend Snippet: LPS binding. We used a chromogenic Limulus amoebocyte assay to obtain binding isotherms for E. coli 0111:B4 lipopolysaccharide. The peptides examined included polymyxin B, LL-37, LL-37 pentamide, RL-37, and rabbit CAP-18 (another LPS binding cathelicidin). The EC50 (i.e., the peptide concentrations that bound 50% of the LPS) are shown and provide an approximate binding constant.

Article Snippet: This difference disappeared when the peptides were studied under low-salt conditions (no added NaCl) and was magnified when the NaCl concentration of the underlay gel was raised to 175 mM (Table ). table ft1 table-wrap mode="anchored" t5 TABLE 2 caption a7 Peptide Mean MEC (μg/ml) ± SEM a S. aureus 930918-3 S. aureus 710A MRSA ATCC 33591 S. epidermidis ATCC 49741 0 mM NaCl LL-37 1.39 ± 0.31 1.25 ± 0.11 1.72 ± 0.33 1.77 ± 0.28 mRL-37 0.98 ± 0.08 1.00 ± 0.10 1.33 ± 0.02 1.39 ± 0.12 LL-37 pentamide 2.42 ± 0.09 2.30 ± 0.27 2.52 ± 0.17 1.88 ± 0.22 100 mM NaCl LL-37 48.2 ± 10.6 16.1 ± 0.29 186 ± 16.7 23.6 ± 1.22 mRL-37 2.81 ± 0.11 ∗ 2.48 ± 0.04 ∗∗ ∗ 4.17 ± 0.30 ∗∗ ∗ 2.40 ± 0.09 ∗∗ ∗ LL-37 pentamide 3.47 ± 0.84 ∗ 2.75 ± 0.20 ∗∗ ∗ 3.41 ± 0.40 ∗∗ ∗ 2.14 ± 0.10 ∗∗ ∗ 175 mM NaCl LL-37 >250 193 ± 57.0 >250 110 ± 42.2 mRL-37 6.49 ± 0.30 ∗∗ ∗ 5.76 ± 0.27 ∗∗ ∗ 11.6 ± 0.90 ∗∗ ∗ 6.92 ± 0.38 ∗∗ ∗ LL-37 pentamide 4.63 ± 0.47 ∗∗ ∗ 4.82 ± 1.03 ∗∗ ∗ 4.69 ± 1.32 ∗∗ ∗ 4.31 ± 0.75 ∗∗ ∗ Open in a separate window a n = 3.

Techniques: Binding Assay