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Literature DB >> 22003494

Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin.

Peng Liu¹, Shuai Zhang, Mei-sha Chen, Qian Liu, Chenxuan Wang, Chen Wang, Yan-Mei Li, Flemming Besenbacher, Mingdong Dong.

Abstract

The pathogenesis of type II diabetes can be linked to cosecreted hIAPP/insulin interacting with cell membranes. Here we investigate the nanostructures by co-assembling hIAPP and insulin on surfaces. By tuning the hIAPP/insulin ratio, atomic force microscopy reveals the resulting nanostructure morphology changes from fibrils to oligomers, to annular. Implications for in vivo studies are discussed. This journal is © The Royal Society of Chemistry 2012

Entities: Disease Gene Species

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Year: 2011 PMID： 22003494 DOI： 10.1039/c1cc14285b

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

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Cited

9 in total

1. Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.

Authors: Shuai Zhang; Maria Andreasen; Jakob T Nielsen; Lei Liu; Erik H Nielsen; Jie Song; Gang Ji; Fei Sun; Troels Skrydstrup; Flemming Besenbacher; Niels C Nielsen; Daniel E Otzen; Mingdong Dong
Journal: Proc Natl Acad Sci U S A Date: 2013-02-06 Impact factor: 11.205

2. Heterotropic Modulation of Amylin Fibrillation by Small Molecules: Implications for Formulative Designs.

Authors: Celimar Sinézia; Luís Maurício T R Lima
Journal: Protein J Date: 2020-02 Impact factor: 2.371

3. Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.

Authors: Shanghao Li; Miodrag Micic; Jhony Orbulescu; Jeffrey D Whyte; Roger M Leblanc
Journal: J R Soc Interface Date: 2012-07-11 Impact factor: 4.118

4. A new strategy to reconcile amyloid cross-seeding and amyloid prevention in a binary system of α-synuclein fragmental peptide and hIAPP.

Authors: Yijing Tang; Dong Zhang; Yonglan Liu; Yanxian Zhang; Yifan Zhou; Yung Chang; Bowen Zheng; Alice Xu; Jie Zheng
Journal: Protein Sci Date: 2021-12-08 Impact factor: 6.725

Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin.

1. Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.

2. Heterotropic Modulation of Amylin Fibrillation by Small Molecules: Implications for Formulative Designs.

3. Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.

4. A new strategy to reconcile amyloid cross-seeding and amyloid prevention in a binary system of α-synuclein fragmental peptide and hIAPP.

5. Repurposing of intestinal defensins as multi-target, dual-function amyloid inhibitors via cross-seeding.

6. Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide.

7. Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis.

8. Real-Time Fast Amyloid Seeding and Translocation of α-Synuclein with a Nanopipette.

9. Nanostructural Differentiation and Toxicity of Amyloid-β25-35 Aggregates Ensue from Distinct Secondary Conformation.