Enzyme-assisted semisynthesis of shortened B26-modified insulins.
The role of the invariant residue B26-tyrosine in determining the structural and biological properties of insulin has been extensively investigated by the use of semisynthetic des-(B27-B30)-insulins with modifications of position B26. Apart from the conventional trypsin-catalyzed peptide bond formation between the C-terminal amino acid ArgB22 of des-(B23-B30)-insulin and synthetic tetrapeptides we elaborated a new approach using des-(B26-B30)-insulin as substrate in alpha-chymotrypsin-mediated syntheses. Results obtained from bioassays and CD-spectroscopy underline the importance of position B26 to the association of the native molecule and to the modulation of structural and hormonal properties of shortened insulins.
Sievert
D
D
Deutsches Wollforschungsinstitut, Aachen, Federal Republic of Germany.
Gattner
H G
HG
Lenz
V
V
Höcker
H
H
D000595:Amino Acid Sequence; D002918:Chymotrypsin / Q000737:chemistry; D006801:Humans; D066298:In Vitro Techniques; D007328:Insulin / Q000031:analogs & derivatives / Q000138:chemical synthesis* / Q000378:metabolism; D011972:Receptor, Insulin / Q000378:metabolism
D007328:Insulin; D011972:Receptor, Insulin; D002918:Chymotrypsin