# Aspects of structural landscape of human islet amyloid polypeptide.

@article{He2014AspectsOS,
title={Aspects of structural landscape of human islet amyloid polypeptide.},
author={Jianfeng He and Jin Dai and Jing Li and Xu-biao Peng and Antti J. Niemi},
journal={The Journal of chemical physics},
year={2014},
volume={142 4},
pages={
045102
}
}
• Published 26 December 2014
• Biology
• The Journal of chemical physics
The human islet amyloid polypeptide (hIAPP) co-operates with insulin to maintain glycemic balance. It also constitutes the amyloid plaques that aggregate in the pancreas of type-II diabetic patients. We have performed extensive in silico investigations to analyse the structural landscape of monomeric hIAPP, which is presumed to be intrinsically disordered. For this, we construct from first principles a highly predictive energy function that describes a monomeric hIAPP observed in a nuclear…
6 Citations

## Tables from this paper

• Physics
Journal of Mathematical Chemistry
• 2018
Parvalbumin (Parv) is a typical protein with EF-hand motifs that play an important role in many physiological processes. We present a novel free energy to model the skeletal C$$_\alpha$$α chain of
• Biology
Journal of Mathematical Chemistry
• 2018
This work developed the novel approach instead of MD, in which the Landau free energy was introduced to describe the protein in term of the skeletal C$$_\alpha$$α chain, in order to simulate the unfolding and folding processes for parvalbumin-$$\beta$$β (Parv).
• Biology, Chemistry
British journal of pharmacology
• 2016
This review explores what is known of the structure–function relationships of amylin and provides insights that can be drawn from the closely related peptide, CGRP, and describes how this information is aiding the development of more potent and stableAmylin mimetics, including peptide hybrids.
• Biology
Chinese Physics B
• 2020
This review will first systematically address the theoretical method of topological soliton, then some successful applications will be displayed, including the thermodynamics simulation of protein folding, the property analysis of dynamic conformations, and the multi-scale simulation scheme.
This thesis is for research or private study purposes only, and the author's right to be identified as the author of this thesis is recognized.
• Biology
• 2016
It is hypothesize that soliton-like quasi-ordered conformations appear as an important intermediate stage in this process of protein folding, to identify possible systematic dynamical patterns of self-organisation that govern protein folding process.

## References

SHOWING 1-10 OF 151 REFERENCES

• Biology, Chemistry
Biochemistry
• 2013
Simulations show that hIAPP forms from trimer to pentamer exhibit high structural stability with well-preserved in-register parallel β-sheet and the U-bend conformation, which could help in the development of novel therapeutic agents to block the formation of toxic hI APP oligomeric species for type 2 diabetes.
• Chemistry, Biology
Journal of the American Chemical Society
• 2009
This paper presents the first experimental evidence of a significant population of beta-hairpin conformers for the IAPP peptide, consistent with a previous suggestion in the literature that beta-sheet-rich oligomers are assembled from orderedbeta-hairpins rather than from coiled structures.
• Biology
The Journal of Biological Chemistry
• 2011
This work developed an approach that combines site-directed spin labeling with continuous wave and pulsed EPR to investigate local secondary structure and to determine the relative orientation of the secondary structure elements with respect to each other.
• Biology, Chemistry
Journal of molecular biology
• 2001
The identification of these principal amyloidogenic sequences and the effects of associated factors provide details on the IAPP aggregation pathway and structure of the peptide in its fibrillar state.
• Biology
The journal of physical chemistry. B
• 2013
Differences in the helicity over residues 7-16 may play an important role in early aggregation, although this region is outside of commonly assumed amyloidogenic region 20-29, and this results provide support for the proposed mechanism of fibril formation based on experimentally observed transient helices in amyloidsogenic peptides.
• Chemistry
Journal of the American Chemical Society
• 2013
These states may facilitate the nucleation of hIAPP aggregation through a significant component of the conformational selection mechanism, because they may increase their populations upon aggregation by promoting hydrophobic interactions and at the same time provide a flat geometry to seed the ordered β-strand packing of the fibrils.
• Biology, Chemistry
PLoS Comput. Biol.
• 2013
A structure-activity relationship (SAR) is proposed in which the functional role of IAPP is carried out by the helix-coil conformation, a structure common to both aggregating and non-aggregating species, and it is proposed that theHelix-hairpin fold is also a possible aggregation prone conformation that would lead normally non-Aggregating variants of I APP to form fibrils under conditions where an external perturbation is applied.
• Biology
Journal of Biological Chemistry
• 2004
Analysis of spin label mobility indicates a high degree of order throughout the peptide, although the N-terminal region is slightly less ordered, and possible similarities with respect to the domain organization and parallelism of Alzheimer's amyloid β peptide fibrils are discussed.
• Biology
J. Chem. Inf. Model.
• 2012
Good agreement of the idealized protofilaments with experimental data for amino acid side chain orientations and geometrical features including the inter-β sheet distance and the prot ofilament radius is shown.