Abstract:
:Insulin and insulin-like growth factor 1 (IGF-1) share high sequence homology, but their folding behaviors are significantly different: insulin folds into one unique thermodynamically controlled structure, while IGF-1 folds into two thermodynamically controlled disulfide isomers. However, the origin of their different folding behaviors is still elusive. The amphioxus insulin-like peptide (ILP) is thought to be the common ancestor of insulin and IGF-1. A recombinant single-chain ILP has been expressed previously, and now its folding behavior is investigated. The folding behavior of ILP shows the characteristics of both insulin and IGF-1. On one hand, two thermodynamically controlled disulfide isomers of ILP have been identified; on the other hand, the content of isomer 1 (its disulfides are deduced identical to those of swap IGF-1) is much less than that of isomer 2 (its disulfides are deduced identical to those of native IGF-1); that is, more than 96% of ILP folds into the native structure. The present results suggest that the different folding behaviors of insulin and IGF-1 are acquired through a bifurcating evolution: the tendency of forming the thermodynamically controlled non-native disulfide isomer is diminished during evolution from ILP to insulin, while this tendency is amplified during evolution from ILP to IGF-1. Moreover, the N-terminal Gln residue of ILP can spontaneously form a pyroglutamate residue, and its cyclization has a significant effect on the folding behavior of ILP: the percentage of isomer 1 is approximately 2-fold that of isomer 1 of the noncyclized ILP; that is, isomer 1 becomes more favored when the N-terminal residue of ILP is cyclized. So, we deduce that the N-terminal residues have a significant effect on the folding properties of insulin, IGF-1, and ILP.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Wang S,Guo ZY,Shen L,Zhang YJ,Feng YMdoi
10.1021/bi0346289subject
Has Abstractpub_date
2003-08-19 00:00:00pages
9687-93issue
32eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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