Circular dichroism (CD) spectroscopy was used to investigate the G-quadruplex DNA structures formed from the insulin-linked polymorphic region (ILPR) and their binding to insulin. We examined the structural variations in three of the most common sequences found in the ILPR and two artificially made variant sequences. CD spectral data from 20-80°C shows the unfolding of the variant sequences occur earlier than the naturally occurring sequences from the ILPR. Thermal melting data show that the more abundant DNA sequences A and B from the ILPR have high melting temperatures, while the less abundant (C) and variant sequences have slightly lower melting temperatures. We have quantified the secondary structural content in insulin upon binding to the various ILPR sequences. While there is a slight decrease in alpha-helical content in insulin upon binding to the ILPR DNA sequences, it was most significant for the ILPR Cv sequence with a concomitant increase in beta strands.

Circular dichroism (CD) spectroscopic study of the insulin-linked polymorphic region

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