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. 2010 Jan 11;285(12):9114–9123. doi: 10.1074/jbc.M109.044297

TABLE 2.

Binding of linear and cyclic isoDGR peptides (acetylated and not acetylated) to integrins as measured by competitive binding assay

Competitor Binding of ac-isoDGR/STV-HRP to
αvβ3
αvβ5
αvβ6
αvβ8
α5β1
na Kib n Ki n Ki n Ki n Ki
nm nm nm nm nm
isoDGR-2C 6 9 ± 2 6 380 ± 108 6 118 ± 39 4 710 ± 68 4 95 ± 33f
ac-isoDGR-2C 5 2 ± 0.4c 5 29 ± 7 4 5 ± 2 3 22 ± 6 3 6 ± 2
isoDGR-2G 3 1086 ± 186d 3 6138 ± 1756 3 256 ± 52 3 7370 ± 820 3 1489 ± 424
ac-isoDGR-2G 3 254 ± 81e 3 845 ± 65 3 163 ± 26 3 878 ± 71 3 226 ± 39

a n, number of independent experiments (each in duplicate).

b Ki: equilibrium dissociation constant of the competitor (mean ± S.E.). Ki was calculated by nonlinear regression analysis of competitive binding data by using the “One site-Fit Ki” equation of the GraphPad Prism Software (GraphPad Software, Version 5.00 San Diego, CA).

c p < 0.05 (ac-isoDGR-2C versus isoDGR-2C).

d p < 0.05 (isoDGR-2G versus isoDGR-2C).

e p < 0.01 (ac-isoDGR-2G versus ac-isoDGR-2C).

f p < 0.05 (α5β1 versus αvβ3).