IAPP, pt 2.

Secondary structure, intrinsic disorders, proIAPP:

Amyloidogenic Propensity of ProIAPP and IAPP in the Presence of Negatively Charged Lipid Bilayers
Suman Jha
Biophysical Journal, Volume 96, Issue 3, Supplement 1, February 2009, Page 93a
(only abstract is free available)


Our CD studies show that the secondary structure content of ProIAPP and IAPP is predominantly unordered with small amounts of ordered secondary structure elements as confirmed by ATR-FTIR spectroscopy. However, in the presence of anionic membranes, ProIAPP forms predominantly α-helices and loops that subsequently transform to intermolecular β-sheet structures. For comparison, IAPP forms intermolecular β-sheets largely via unordered and loop structures.

The ATR-FTIR and fluorescence spectroscopy studies performed also reveal that ProIAPP has a higher amyloidogenic propensity in the presence of negatively charged membranes, but is still less amyloidogenic than IAPP.