. 2021 Nov 5;32(12):2766–2776. doi: 10.1021/jasms.1c00206

Table 1. Comparison of Conditional Cu(II) Binding Constants of the Studied Peptides at pH = 7.4 (^CK_7.4), Compared to These Constants Determined Previously by Other Methods and Published^a.

peptide sequence (name)	published log ^CK_7.4^b	log K_d ± SD from serial dilution ESI-MS experiment in this study	log ratio log K_d (ESI-MS) – log ^CK_7.4 (published)	range of concentrations in this study (μM)
DTHFPI-NH₂(hepc6)	14.7^c	7.6 ± 0.7	–7.1	100–0.01
MNH-NH₂	14.5^d	6.3 ± 0.4	–8.2	100–2
FRHDSG (Aβ4–9)	14.2^e	6.9 ± 0.9	–5.3	100–1
FRHDSGYEVHHQK-NH₂ (Aβ4–16)	13.5^f	7.0 ± 0.2	–6.5	100–0.5
MDH-NH₂	13.1^d	7.1 ± 0.6	–6.0	100–1
GGH	12.2^g	6.0 ± 0.5	–6.2	100–10

Standard deviation of ESI-MS experimental values are given in parentheses. Logarithmic values are given for better clarity. The published log ^CK_7.4 values were determined by potentiometry and corroborated by spectroscopic methods.

The SD values were considerably less than 0.1 log unit in all cases.

Reference (63).

Reference (64).

Reference (65).

Reference (6).

Reference (21).

Table 1. Comparison of Conditional Cu(II) Binding Constants of the Studied Peptides at pH = 7.4 (CK7.4), Compared to These Constants Determined Previously by Other Methods and Publisheda.

Table 1. Comparison of Conditional Cu(II) Binding Constants of the Studied Peptides at pH = 7.4 (^CK_7.4), Compared to These Constants Determined Previously by Other Methods and Published^a.