TY - JOUR
T1 - Interaction of amylin species with transition metals and membranes
AU - Alghrably, Mawadda
AU - Czaban, Iwona
AU - Jaremko, Lukasz
AU - Jaremko, Mariusz
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: Authors would like to thank King Abdullah University of Science and Technology (KAUST) for financial support.
PY - 2018/11/10
Y1 - 2018/11/10
N2 - Islet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide hormone that is secreted by pancreatic islet β-cells. Amylin is complementary to insulin in regulating and maintaining blood glucose levels in the human body. The misfolding and aggregation of amylin is primarily associated with type 2 diabetes mellitus, which is classified as an amyloid disease. Recently, the interactions between amylin and specific metal ions, e.g., copper(II), zinc(II), and iron(II), were found to impact its performance and aggregation processes. Therefore, the focus in this review will be on how the chemistry and structural properties of amylin are affected by these interactions. In addition, the impact of amylin and other amyloidogenic peptides interacting with metal ions on the cell membranes is discussed. In particular, recent studies on the interactions of amylin with copper, zinc, iron, nickel, gold, ruthenium, and vanadium are discussed.
AB - Islet Amyloid Polypeptide (IAPP), also known as amylin, is a 37-amino-acid peptide hormone that is secreted by pancreatic islet β-cells. Amylin is complementary to insulin in regulating and maintaining blood glucose levels in the human body. The misfolding and aggregation of amylin is primarily associated with type 2 diabetes mellitus, which is classified as an amyloid disease. Recently, the interactions between amylin and specific metal ions, e.g., copper(II), zinc(II), and iron(II), were found to impact its performance and aggregation processes. Therefore, the focus in this review will be on how the chemistry and structural properties of amylin are affected by these interactions. In addition, the impact of amylin and other amyloidogenic peptides interacting with metal ions on the cell membranes is discussed. In particular, recent studies on the interactions of amylin with copper, zinc, iron, nickel, gold, ruthenium, and vanadium are discussed.
UR - http://hdl.handle.net/10754/629864
UR - https://www.sciencedirect.com/science/article/pii/S0162013418304409
UR - http://www.scopus.com/inward/record.url?scp=85056778928&partnerID=8YFLogxK
U2 - 10.1016/j.jinorgbio.2018.11.004
DO - 10.1016/j.jinorgbio.2018.11.004
M3 - Article
C2 - 30468944
SN - 0162-0134
VL - 191
SP - 69
EP - 76
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
ER -
