A dimer model of human calcitonin13‐32 forms an α‐helical structure and robustly aggregates in 50% aqueous 2,2,2‐trifluoroethanol solution

We report that a dimer model of human calcitonin13‐32 (hCT13‐32) aggregated to a greater degree than native hCT under aqueous TFE conditions. Analyses using circular dichroism spectroscopy, thioflavine‐T binding assays and atomic force microscopy suggest that the α‐helical portion of hCT is important for initiation of the aggregation process, which yields long fibrils. Our findings could potentially serve as the basis for development of novel hCT derivatives that could be utilized for treatment of hypercalcemia.

Source: Journal of Peptide Science - May 29, 2016 Category: Biochemistry Authors: Hiroyuki Kawashima, Mei Katayama, Ryota Yoshida, Kenichi Akaji, Akiko Asano, Mitsunobu Doi Tags: Research Article Source Type: research