Peptides are attracting a growing interest for therapeutic applications in biomedicine. In Parkinson's disease (PD), different human endogenous peptides have been associated with beneficial effects, including protein aggregation inhibition, reduced inflammation, or the protection of dopaminergic neurons. Such effects seem to be connected to the spatial arrangement of peptide side chains, and many of these human molecules share common conformational traits, displaying a distinctive amphipathic and cationic helical structure, which is believed to be crucial for their activities. This review delves into the relationship between these structural properties and the current evidence connecting biogenic peptides to the amelioration of PD symptoms. We discuss their implications in the disease, the different mechanisms of action, their state of validation, and their therapeutic potential.
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http://dx.doi.org/10.1002/pro.70020 | DOI Listing |
PeerJ
December 2024
Department of Microbiology and Parasitology, Faculty of Medical Science, Naresuan University, Muang, Phitsanulok, Thailand.
Background: poses a significant public health threat. Phage-encoded antimicrobial peptides (AMPs) have emerged as promising candidates in the battle against antibiotic-resistant .
Methods: Antimicrobial peptides from the endolysin of bacteriophage were designed from bacteriophage vB_AbaM_PhT2 and vB_AbaAut_ChT04.
Protein Sci
January 2025
Institut de Biotecnologia i de Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.
Peptides are attracting a growing interest for therapeutic applications in biomedicine. In Parkinson's disease (PD), different human endogenous peptides have been associated with beneficial effects, including protein aggregation inhibition, reduced inflammation, or the protection of dopaminergic neurons. Such effects seem to be connected to the spatial arrangement of peptide side chains, and many of these human molecules share common conformational traits, displaying a distinctive amphipathic and cationic helical structure, which is believed to be crucial for their activities.
View Article and Find Full Text PDFBiophys Chem
December 2024
Karlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany; KIT, Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany. Electronic address:
KIA peptides were designed as a series of cationic antimicrobial agents of different lengths, based on the repetitive motif [KIAGKIA]. As amphiphilic helices, they tend to bind initially to the surface of lipid membranes. Depending on the conditions, they are proposed to flip, insert and form toroidal pores, such that the peptides are aligned in a transmembrane orientation.
View Article and Find Full Text PDFMicrobiol Spectr
January 2025
Department of Clinical Laboratory, Key Laboratory of Clinical Laboratory Diagnosis and Translational Research of Zhejiang Province, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China.
Unlabelled: Carbapenem-resistant (CRKP) and (CREC) are frequently detected in clinical settings, restricting the use of carbapenems. Therefore, there is an urgent need for new antimicrobial strategies to address infections caused by CRKP and CREC. This study investigated the antibacterial, anti-biofilm, and anti-inflammatory effects of the cationic antimicrobial peptide Hs02, along with its potential antimicrobial mechanisms against CRKP and CREC.
View Article and Find Full Text PDFPharmaceutics
November 2024
Grupo Genética, Regeneración y Cáncer, Facultad de Ciencias Exactas y Naturales, Instituto de Biología, Universidad de Antioquia, Medellín 050010, Colombia.
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