TABLE 1.

ACE analysis of the interaction between tripeptides and HIV-1 p24 and human hemoglobin (used as control protein)a

TripeptideMigration time t1 (min) in the absence of:Migration time t2 (min) in the presence of:RDM $$mathtex$$\(\left(100{\,}{\cdot}{\,}\frac{\mathit{u}_{1}{-}\mathit{u}_{2}}{\mathit{u}_{1}}\right)\)$$mathtex$$b
p24Hemoglobinp24Hemoglobinp24Hemoglobin
pH 6.8
    RQG-NH23.10ND3.36ND7.75ND
    GPG-NH23.303.433.463.444.580.3
    ALG-NH24.284.314.564.326.10.2
    ALG-OHc
    GPG-OHc
pH 7.5
    RQG-NH23.76ND4.21ND10.6ND
    GPG-NH24.063.824.503.839.80.3
    ALG-NH25.585.386.195.409.80.4
    ALG-OHc
    GPG-OHc
pH 8.2
    RQG-NH23.69ND3.93ND6.1ND
    GPG-NH27.15ND7.94ND9.9ND
    ALG-NH2c
    ALG-OH6.516.416.546.430.50.3
    GPG-OH8.918.908.938.920.20.2
  • a The length of the protein zone was 4.7 or 14.0 (for pH 8.2) mm long in each run. The values are averages of two or three measurements in which the run-to-run reproducibility was higher than 98%. Note that the series of runs with p24 were performed in one capillary and those with hemoglobin in another. The coating used to suppress electroendosmotic flow and adsorption vary somewhat from one capillary to another. A few percentage variations are expected and tolerable. ND, not determined.

  • b The equation (l·L)/(t·V) reveals the relationship between the mobility (u) and the migration time (t) (l is the effective length and L is the total length of the capillary, respectively, and V is the applied voltage). Using this relationship, it is easy to show that RDM can be written as (t2t1)/t2·100.

  • c Electrophoretic mobility ≈ 0.