Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus

Autor: Lucie Caillon, Anais R. F. Hoffmann, Alexandra Botz, Lucie Khemtemourian

Publikováno v: Journal of Diabetes Research, Vol 2016 (2016)

Human islet amyloid polypeptide (hIAPP) is the major component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus (T2DM). Mature hIAPP, a 37-aa peptide, is natively unfolded in its monomeric state but for

Externí odkaz: https://doaj.org/article/9939481e49624538977a92288fe46aa6

Time dependence of NMR observables reveals salient differences in the accumulation of early aggregated species between human islet amyloid polypeptide and amyloid-β

Autor: Olivier Lequin, Ludovic Carlier, Pierre-Alexandre Spath, Anais R. F. Hoffmann, Lucie Khemtémourian, Lucie Caillon, Lilian Shadai Salazar Vazquez

Publikováno v: Physical Chemistry Chemical Physics
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2018, 20 (14), pp.9561-9573. ⟨10.1039/C7CP07516B⟩

International audience; Type 2 diabetes mellitus and Alzheimer's disease are characterized by the accumulation of fibrillar amyloid deposits consisting mainly of islet amyloid polypeptide (IAPP) and amyloid-b (Ab), respectively. Fibril formation is a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f19e095b4ef722b506835f51795d714e
https://hal.sorbonne-universite.fr/hal-01840142

Designed Glycopeptidomimetics Disrupt Protein–Protein Interactions Mediating Amyloid β-Peptide Aggregation and Restore Neuroblastoma Cell Viability

Autor: Katia Fabiana Fera, Olivier Lequin, David Allsop, Jean-Louis Soulier, Benoit Crousse, Nicolo Tonali, Dimitri Brinet, Mark Taylor, Lucie Khemtémourian, Isabelle Correia, Anais R. F. Hoffmann, Sandrine Ongeri, Yasmine Iacone, Julia Kaffy, Myriam Taverna

Publikováno v: Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 2016, 59 (5), pp.2025-2040. ⟨10.1021/acs.jmedchem.5b01629⟩
Journal of Medicinal Chemistry, American Chemical Society, 2016, 59 (5), pp.2025-2040. 〈10.1021/acs.jmedchem.5b01629〉
Journal of Medicinal Chemistry, 2016, 59 (5), pp.2025-2040. ⟨10.1021/acs.jmedchem.5b01629⟩

International audience; How anti-Alzheimer’s drug candidates that reduce amyloid 1–42 peptide fibrillization interact with the most neurotoxic species is far from being understood. We report herein the capacity of sugar-based peptidomimetics to i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51f19a813c4432451068411b21bbe840
https://hal.archives-ouvertes.fr/hal-01303733

(R)-α-trifluoromethylalanine containing short peptide in the inhibition of amyloid peptide fibrillation

Autor: Alexandra, Botz, Vincent, Gasparik, Emmanuelle, Devillers, Anais R F, Hoffmann, Lucie, Caillon, Evelyne, Chelain, Olivier, Lequin, Thierry, Brigaud, Lucie, Khemtemourian

Publikováno v: Biopolymers. 104(5)

The extracellular deposition of insoluble amyloid fibrils resulting from the aggregation of the amyloid-β (Aβ) is a pathological feature of neuronal loss in Alzheimer's disease (AD). Numerous small molecules have been reported to interfere with the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5863a8b31ebdbc51b033fb8fa068d799
https://pubmed.ncbi.nlm.nih.gov/25968595