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. Author manuscript; available in PMC: 2014 Mar 5.
Published in final edited form as: Biochemistry. 2012 Apr 15;51(16):3445–3450. doi: 10.1021/bi2016519

Table 1.

Binding Affinities of the Charged-to-Uncharged γ′ Peptides

Peptide Sequence Kd (μM) (mean ± standard error of the mean) P value (compared to wild-type)*
Wild-type PEHPAETEpYDSLpYPEDDL 0.440 ± 0.011
#1 PQHPAETEpYDSLpYPEDDL 0.441 ± 0.016 1.00
#2 PEHPAQTEpYDSLpYPEDDL 0.485 ± 0.011 0.46
#3 PEHPAETQpYDSLpYPEDDL 0.541 ± 0.010 0.025
#4 PEHPAETE YDSLpYPEDDL 0.583 ± 0.011 0.008
#5 PEHPAETEpYNSLpYPEDDL 0.705 ± 0.011 <0.001
#6 PEHPAETEpYDSL YPEDDL 0.702 ± 0.021 0.018
#7 PEHPAETEpYDSLpYPQDDL 0.582 ± 0.018 0.073
#8 PEHPAETEpYDSLpYPENDL 0.608 ± 0.019 0.053
#9 PEHPAETEpYDSLpYPEDNL 0.465 ± 0.010 1.00
#10 PEHPAETE YNSL YPEDDL
#11 PQHPAQTQpYDSLpYPQNNL
#12 PQHPAQTQpYDSLpYPEDDL 1.968 ± 0.025 <0.001
#13 PEHPAETEpYDSLpYPQNNL 3.189 ± 0.034 0.002

BIAevaluation software was used to calculate affinity constants (Kd) based on a 1:1 Langmuir binding model. Standard error of the mean was calculated from triplicate determinations.

*

P values were adjusted for multiple comparisons using Bonferroni correction.

This potential individual and institutional conflict of interest has been reviewed and managed by OHSU.