NDLI: Interactions of the N-terminal domain of human islet amyloid polypeptide with lipid membranes: the effect of cholesterol

Content Provider	Royal Society of Chemistry (RSC)
Author	Guan, Liping Lu, Tong Li, Zhengqiang Li, Haichao Li, Yang Li, Fei
Copyright Year	2016
Abstract	The 1–19 region of human islet amyloid polypeptide (hIAPP1–19) is a dominating factor causing the interaction between hIAPP and membrane. It contains a short sequence RLANFLV that fulfils the amino-acid arrangement of the inversed cholesterol recognition amino-acid consensus (CARC) and may mediate a direct contact of hIAPP with cholesterol. In this study, we focused on the interaction of hIAPP1–19 with the lipid membrane composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and cholesterol, and examined the role of the CARC motif in the peptide–membrane interaction. Using differential scanning calorimetry, 31P-NMR spectroscopy, 1H-NMR titration measurement and dye leakage assay, we demonstrated that hIAPP1–19 interacts with DPPC vesicles more strongly in the presence of cholesterol than it does in the absence of cholesterol. The peptide–membrane interaction promotes the domain segregation of the raft-containing membrane. The peptide is more disruptive to the cholesterol-containing membrane than it is to the cholesterol-depleted membrane. The substitution of the residue Phe at position 15 of hIAPP1–19 by Leu leads to a distinct decrease in the peptide–membrane interaction in the presence of cholesterol, but the effect of the residue substitution on the peptide–membrane interaction is very small in the absence of cholesterol. The circular dichroism data indicated that a conversion of the structure from a random coil to an α-helix is induced by cholesterol for both peptides and the structural conversion is more Chol-dependent for the wild-type peptide than the F15L variant. Our findings suggest that cholesterol could facilitate the insertion and aggregation of the N-terminal domain of hIAPP in the membrane, and the phenylalanine in the CARC motif could be involved in the interaction of the N-terminal domain with Chol.
Starting Page	96837
Ending Page	96846
Page Count	10
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	6
Issue Number	99
Journal	RSC Advances
DOI	10.1039/c6ra19714k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Differential scanning calorimetry Spectroscopy Chol Alpha helix Phenylalanine Amylin Staining Cholesterol Phosphocholine Circular dichroism CARC N-terminus Direct Contact Lipid bilayer Titration Random coil Peptide DPPC Dipalmitoylphosphatidylcholine
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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