LysPro insulin

Pillion, D.J., S. Hosmer, and E. Meezan. 1998. Dodecylmaltoside-mediated nasal and ocular absorption of lyspro-insulin Independence of surfactant action from peptide multimer dissociation. Pharm Res 15 1641. 

Fig. 10 CD spectra for (a) the Cu(II)-D-histidine host complex and for the mixed ligand complexes with (b) bovine insulin, (c) human insulin, (d) porcine insulin, and (e) human LysPro insulin.

Zwickl CM, Smith HW, Zimmerman JL, Wierda D. Immunogenicity of biosynthetic human LysPro insulin compared to native-sequence human and purified porcine insulins in rhesus monkeys immunized over a 6-week period. Arzneimittelforschung 1995 45 524-528. 

More recently, manipulation of the structure of the B-chain, aiming at decreasing the potential for P-sheet interactions of the peptide backbone between insulin monomers, has also resulted in insulins with decreased tendency to self-associate. Examples of such analogs are the LysPro insulin (Brems et al, 1992), in which the B28 and B29 residues are interchanged, as is the case in insulin-like growth factor-I, and analogs characterized by deletion of one of the amino acid residues in the B25 B28 sequence (Balschmidt and Brange, 1992). 

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