Insulin glulisine in the management of diabetes

Figures & data

Figure 1 The amino acid sequence of human insulin and rapid-acting insulin analogs. Pink circles: amino acid residues involved in dimer formation. Blue circles: amino acid residues involved in hexamer formation. Arrow: amino acid residues involved in binding with the insulin receptor. A) human insulin, B) insulin lispro, C) insulin aspart, and D) insulin glulisine.

Table 1 Comparison of regular human insulin and rapid-acting insulin analogs

			Human insulin	Insulin lispro	Insulin aspart	Insulin glulisine
Insulin action	Onset	min	30–60	5–15	5–15	5–15
	Peak	h	2–3	0.5–1.5	0.5–1.5	0.5–1.5
	Cmax	μg/L	0.6–2.5	0.8–4.1
		pmol/L	195–260		341–506
		mU/L	40 ± 10			73 ± 16
		ratio	100	222	175	183
	Duration	hr	6–10	4–5	4–5	4–5
Excipients	Zinc		+	+	+	−
	Polysorbate 20		−	−	−	+
	Trometamol		−	−	−	+
Receptor binding and mitogenic potencies	Insulin receptor affinity (%)		100	84 ± 6	92 ± 6	68–71
	Insulin receptor off-rate (%)		100	100 ± 11	81 ± 8	n.a.
	Metabolic potency (%)		100	82 ± 3	101 ± 2	44–45
	IGF-1 receptor affinity (%)		100	156 ± 16	81 ± 9	16.2
	Mitogenic potency (%)		100	66 ± 10	58 ± 22	Nearly 100