4.6 Editorial Material

LL-37 and CsgC exemplify the crosstalk between anti-amyloid, antimicrobial, and anti-biofilm protein activities

相关参考文献

注意:仅列出部分参考文献,下载原文获取全部文献信息。
Article Chemistry, Multidisciplinary

Remodeling of the Fibrillation Pathway of α-Synuclein by Interaction with Antimicrobial Peptide LL-III

Rosario Oliva et al.

Summary: Liquid-liquid phase separation (LLPS) is a key mechanism for intracellular organization and has implications in various medical conditions. The antimicrobial peptide LL-III can interact with alpha-synuclein to stabilize droplets and prevent fibril formation, showcasing potential for disease intervention.

CHEMISTRY-A EUROPEAN JOURNAL (2021)

Article Multidisciplinary Sciences

Genome-wide screen identifies curli amyloid fibril as a bacterial component promoting host neurodegeneration

Chenyin Wang et al.

Summary: This study reveals the critical role of gut microbiota in regulating neurodegenerative diseases, particularly through influencing the formation and aggregation of amyloid fibrils. This provides a new research direction for the treatment of neurodegenerative diseases.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2021)

Article Multidisciplinary Sciences

α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity

Jaime Santos et al.

Summary: Researchers have identified a class of peptides that can bind toxic α-synuclein oligomers and amyloid fibrils without interfering with monomeric functional protein, preventing further aggregation and associated cell damage.

NATURE COMMUNICATIONS (2021)

Article Chemistry, Multidisciplinary

Antimicrobial α-defensins as multi-target inhibitors against amyloid formation and microbial infection

Yanxian Zhang et al.

Summary: The study proposed a novel anti-amyloid and antimicrobial hypothesis using two host-defense antimicrobial peptides containing beta-rich structures to inhibit amyloid aggregation and microbial infection while retaining antimicrobial activity. The discovery of these peptides greatly expands the therapeutic potential of antimicrobial peptides as multi-target amyloid inhibitors for better understanding and treating amyloid diseases.

CHEMICAL SCIENCE (2021)

Article Chemistry, Multidisciplinary

The Human Host-Defense Peptide Cathelicidin LL-37 is a Nanomolar Inhibitor of Amyloid Self-Assembly of Islet Amyloid Polypeptide (IAPP)

Valentina Armiento et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2020)

Article Cell Biology

Functional Amyloids

Daniel Otzen et al.

COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2019)

Article Multidisciplinary Sciences

Inhibition of curli assembly and Escherichia coli biofilm formation by the human systemic amyloid precursor transthyretin

Neha Jain et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017)

Article Multidisciplinary Sciences

Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones

Jonathan D. Taylor et al.

SCIENTIFIC REPORTS (2016)

Article Biochemistry & Molecular Biology

The Bacterial Curli System Possesses a Potent and Selective Inhibitor of Amyloid Formation

Margery L. Evans et al.

MOLECULAR CELL (2015)