The Human Host‐Defense Peptide Cathelicidin LL‐37 is a Nanomolar Inhibitor of Amyloid Self‐Assembly of Islet Amyloid Polypeptide (IAPP)
Abstract: Amyloid self‐assembly of islet amyloid polypeptide (IAPP) is linked to pancreatic inflammation, β‐cell degeneration, and the pathogenesis of type 2 diabetes (T2D). The multifunctional host‐defence peptides (HDPs) cathelicidins play crucial roles in inflammation. Here, we show that the antimicrobial and immunomodulatory polypeptide human cathelicidin LL‐37 binds IAPP with nanomolar affinity and effectively suppresses its amyloid self‐assembly and related pancreatic β‐cell damage in vitro. In addition, we identify key LL‐37 segments that mediate its interaction with IAPP. Our results suggest a possible protective role for LL‐37 in T2D pathogenesis and offer a molecular basis for the design of LL‐37‐derived peptides that combine antimicrobial, immunomodulatory, and T2D‐related anti‐amyloid functions as promising candidates for multifunctional drugs.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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The Human Host‐Defense Peptide Cathelicidin LL‐37 is a Nanomolar Inhibitor of Amyloid Self‐Assembly of Islet Amyloid Polypeptide (IAPP) ; volume:59 ; number:31 ; year:2020 ; pages:12837-12841 ; extent:5
Angewandte Chemie / International edition. International edition ; 59, Heft 31 (2020), 12837-12841 (gesamt 5)
- Creator
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Armiento, Valentina
Hille, Kathleen
Naltsas, Denise
Lin, Jennifer S.
Barron, Annelise E.
Kapurniotu, Aphrodite
- DOI
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10.1002/anie.202000148
- URN
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urn:nbn:de:101:1-2022061409022961981568
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:37 AM CEST
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Associated
- Armiento, Valentina
- Hille, Kathleen
- Naltsas, Denise
- Lin, Jennifer S.
- Barron, Annelise E.
- Kapurniotu, Aphrodite
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Identification of key residues of the cross-interaction of islet amyloid polypeptide (IAPP) with β-amyloid peptide (Aβ), its amyloid self-assembly and its bioactivity
Identification and characterization of IAPP derived inhibitors of cytotoxic self-assembly and amyloidogenesis of islet amyloid polypeptide (IAPP) and ß-amyloid [beta amyloid] peptide (Aß) [A beta]
Zinc and iron dynamics in human islet amyloid polypeptide-induced diabetes mouse model
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Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo
Contraction of human brain vascular pericytes in response to islet amyloid polypeptide is reversed by pramlintide
Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide
Islet amyloid polypeptide cross-seeds tau and drives the neurofibrillary pathology in Alzheimer’s disease
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
Identification of key residues of the cross-interaction of islet amyloid polypeptide (IAPP) with β-amyloid peptide (Aβ), its amyloid self-assembly and its bioactivity
Identification and characterization of IAPP derived inhibitors of cytotoxic self-assembly and amyloidogenesis of islet amyloid polypeptide (IAPP) and ß-amyloid [beta amyloid] peptide (Aß) [A beta]
Zinc and iron dynamics in human islet amyloid polypeptide-induced diabetes mouse model
Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice
Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo
Contraction of human brain vascular pericytes in response to islet amyloid polypeptide is reversed by pramlintide
Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
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