Table 1.
Binding properties of full‐length chemokines and peptides derived from their N‐terminal regions towards CXCR4 and ACKR3
Name | Sequence | Binding competition | |
---|---|---|---|
CXCR4 | ACKR3 | ||
pIC50 ± SEM | pIC50 ± SEM | ||
CXCL12 | 7.89 ± 0.04 | 8.74 ± 0.07 | |
CXCL121–17 | KPVSLSYRCPCRFFESH | ~4.00 | 5.39 ± 0.10 |
CXCL121–9 | KPVSLSYRS | <3.00 | 5.05 ± 0.13ns |
(CXCL121–9)2 | (KPVSLSYRC)2 | 5.31 ± 0.16 | 5.65 ± 0.09* |
CXCL121–17D | KPVSLSYRCPCRFFESH | ~4.00 | <4.00 |
CXCL122–17 | ‐ PVSLSYRCPCRFFESH | ~4.00 | 5.23 ± 0.25ns |
CXCL121–17/P2G | KGVSLSYRCPCRFFESH | <4.00 | 4.22 ± 1.19ns |
vCCL2 | 7.70 ± 0.06 | 7.47 ± 0.07 | |
vCCL21–21 | LGASWHRPDKCCLGYQKRPLP | 5.71 ± 0.24 | 5.77 ± 0.13 |
vCCL21–11 | LGASWHRPDKS | ~4.00 | 5.27 ± 0.24ns |
(vCCL21–11)2 | (LGASWHRPDKC)2 | 6.67 ± 0.06 | 5.59 ± 0.13ns |
vCCL21–21 D | LGASWHRPDKCCLGYQKRPLP | 6.21 ± 0.21ns | ~4.00 |
CXCL11 | <6.00 | 8.45 ± 0.03 | |
CXCL111–17 | FPMFKRGRCLCIGPGVK | <4.52a | 5.46 ± 0.12a |
CXCL111–9 | FPMFKRGRS | ND | 5.09 ± 0.13ns |
(CXCL111–9)2 | (FPMFKRGRC)2 | ND | 6.03 ± 0.14* |
CXCL111–17D | FPMFKRGRCLCIGPGVK | ND | 5.06 ± 0.12*, a |
CXCL112–17 | ‐ PMFKRGRCLCIGPGVK | ND | <4.52a |
CXCL111–17/P2G | FGMFKRGRCLCIGPGVK | ND | 6.72 ± 0.09*, a |
CXCL10 | <6.00 | <6.00 | |
CXCL101–17 | VPLSRTVRCTCISISNQ | <4.52a | <4.52*, a |
Binding competition studies with fluorescently labelled CXCL12 were performed in U87 cells (n = 5). Peptides 1‐17 (for CXCL12 and CXCL11) and 1‐21 (for vCCL2) were considered as the standard, reference peptides and monomeric mutant peptides were compared with these. Where dimeric peptides were assessed, these were compared with their corresponding monomeric peptides.
P < 0.05, significantly different from standard peptides or from monomeric peptides; ns, not significant, P > 0.05.
Highest concentration tested 30 μM. ND: not determined.