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A genome-inspired DNA ligand for the affinity capture of insulin and insulin-like growth factor-2

✍ Scribed by Junfeng Xiao; Jennifer A. Carter; Kimberley A. Frederick; Linda B. McGown

Book ID
102926150
Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
956 KB
Volume
32
Category
Article
ISSN
1615-9306

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✦ Synopsis

Abstract

The insulin‐linked polymorphic region (ILPR) of the human insulin gene contains tandem repeats of similar G‐rich sequences, some of which form intramolecular G‐quadruplex structures in vitro. Previous work showed affinity binding of insulin to an intramolecular G‐quadruplex formed by ILPR variant a. Here, we report on interactions of insulin and the highly homologous insulin‐like growth factor‐2 (IGF‐2) with ILPR variants a, h, and i. Circular dichroism indicated intramolecular G‐quadruplex formation for variants a and h. Affinity MALDI MS and surface plasmon resonance were used to compare protein capture and binding strengths. Insulin and IGF‐2 exhibited high binding affinity for variants a and h but not i, indicating the involvement of intramolecular G‐quadruplexes. Interaction between insulin and variant a was unique in the appearance of two binding interactions with K~D~ ∼︁ 10^–13^ M and K~D~ ∼︁ 10^–7^ M, which was not observed for insulin with variant h (K~D~ ∼︁ 10^–8^ M) or IGF‐2 with either variant (K~D~s ∼︁ 10^–9^ M). The results provide a basis for the design of DNA binding ligands for insulin and IGF‐2 and support a new approach to discovery of DNA affinity binding ligands based on genome‐inspired sequences rather than the traditional combinatorial selection route to aptamer discovery.

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