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. Author manuscript; available in PMC: 2013 Dec 1.
Published in final edited form as: Curr Diab Rep. 2012 Dec;12(6):697–704. doi: 10.1007/s11892-012-0318-z

Table 1.

Current Insulin Analogs and Modes of Actiona

Analog Modification Mechanism
A
Lispro (Humalog®)
Eli Lilly and Co.		 ProB28 → Lys
LysB29 → Pro		 IGF-I-related motif impairs dimerization
Aspart (NovoLog®)
Novo-Nordisk		 ProB28 → Asp Charge repulsion at dimer interface
Glulisine (Apidra®)
Sanofi-Aventis		 AsnB3 → Lys
LysB29 → Glu		 Decreased zinc-free self-association
B
Glargine (Lantus®)
Sanofi-Aventis		 ArgB31-ArgB32 tag
AspA21 → Gly		 Shift in pI to pH 7 leads to isoelectric precipitation on injection
Detemir (Levemir®)
Novo-Nordisk		 Modification of LysB29 by a tethered fatty acid Stabilization of hexamer and binding to serum albumin
C
Insulin degludec Novo-Nordisk Modification of LysB29 by a dicarboxylic acid Allosteric assembly of a linear T6 polymer and albumin binding
LY2605541
Eli Lilly and Co.		 PEGylation of LysB28 in insulin lispro Increased hydrodynamic radius
a

Panel A lists rapid-acting analogs employed in prandial regimens and in insulin pumps. Panel B describes basal insulin analogs with protracted action. Panel C lists novel basal insulin analogs undergoing Phase 3 clinical trials; PEG, polyethylene glycol.