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. 2020 Nov 5;117(47):29618–29628. doi: 10.1073/pnas.2010908117

Table 3.

Self-association properties of insulin analogs

Analog t1/2 Hexamer dissociation* (min ± SD) Calculated molecular mass by SEC (kDa ± fit error)
Human insulin (ins) 7.7 ± 1.3 6.8 ± 3.1
Ins lispro 4.6 ± 0.3 4.2 ± 2.0
OrnB29 -ins§ 8.6 ± 1.3 6.6 ± 3.0
TyrB24, OrnB29-ins 7.6 ± 0.3 4.7 ± 2.2
*

t1/2 and SD were calculated from three replicates; two-sided P values for lispro, OrnB29-ins, and TyrB24, OrnB29-ins against t1/2 of human insulin were 0.06, 0.44, and 0.91, respectively.

Proteins were made 0.6 mM in a buffer containing ZnCl2 at a ratio of two zinc ions per insulin hexamer and applied to SEC column (Materials and Methods); masses were calculated based on protein standards (SI Appendix, Fig. S19B).

Insulin lispro (KP-insulin) contains substitutions ProB28→Lys (K) and LysB29→Pro (P).

§

Substitution LysB29→Orn was introduced for synthetic convenience.