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Background: Antimicrobial peptides (AMP) play a pivotal role in innate host defense and in immune response. The delineation of new MS-based profiling tools, which are able to produce panels of AMP of the nasal fluid (NF), may be attractive for the discovery of new potential diagnostic markers of respiratory disorders.
Methods: Swabs collected NF from healthy patients and from patients with respiratory disorders. We used a fast procedure based on mesoporous silica particles (MPS) to enrich NF in its AMP component in combination with MALDI-TOF/TOF MS as a key tool for rapidly analyzing clinical samples.
Results: Reproducible MS peptide fingerprints were generated for each subject and several AMP were detected including (Human Neutrophil Peptides) HNPs, Statherin, Thymosin-β4, Peptide P-D, II-2, β-MSP, SLPI, Lysozyme-C, and their proteo-forms. In particular, Statherin, Thymosin-β4, and Peptide P-D were accurately identified by direct MS/MS sequencing. Examples of applicability of this tool are shown. AMP fingerprints were obtained before and after a nasal polypectomy as well as before and post-treatment with azelastine/fluticasone in one case of allergic rhinitis.
Conclusion: The potential of our platform to be implemented by new mesoporous materials for capturing a wider picture of AMP might offer an amazing opportunity for diagnostic clinical studies on individual and population scales.
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http://dx.doi.org/10.3390/ijms19124005 | DOI Listing |
Nanoscale Horiz
September 2025
Programmable Biomaterials Laboratory, Institute of Materials, Interfaculty Bioengineering Institute, School of Engineering, Ecole Polytechnique Fédérale Lausanne, Lausanne, 1015, Switzerland.
The nanoscale spatial arrangement of T cell receptor (TCR) ligands critically influences their activation potential in CD8 T cells, yet a comprehensive understanding of the molecular landscape induced by engagement with native peptide-MHC class I (pMHC-I) remains incomplete. Using DNA origami nanomaterials, we precisely organize pMHC-I molecules into defined spatial configurations to systematically investigate the roles of valencies, inter-ligand spacings, geometric patterns, and molecular flexibility in regulating T cell function. We find that reducing the inter-ligand spacing to ∼7.
View Article and Find Full Text PDFMol Biol Rep
September 2025
Prevention of Metabolic Disorders Research Center, Research Institute for Endocrine Sciences, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
FASEB Bioadv
September 2025
Kobilka Institute of Innovative Drug Discovery, School of Medicine The Chinese University of Hong Kong Shenzhen Guangdong China.
Formyl peptide receptor 1 (FPR1) is a G protein-coupled receptor (GPCR) that mediates chemotaxis and bactericidal activities in phagocytes. The monoclonal antibody 5F1 is generated against full-length FPR1 and used widely for detection of FPR1 expression. This study aimed to characterize 5F1 for its functions.
View Article and Find Full Text PDFEMBO J
September 2025
School of Life and Environmental Sciences, Faculty of Science, The University of Sydney, Sydney, NSW, Australia.
Insulin resistance is a heritable risk factor for many chronic diseases; however, the genetic drivers remain elusive. In seeking these, we performed genetic mapping of insulin sensitivity in 670 chow-fed Diversity Outbred in Australia (DOz) mice and identified a genome-wide significant locus (QTL) on chromosome 8 encompassing 17 defensin genes. By taking a systems genetics approach, we identified alpha-defensin 26 (Defa26) as the causal gene in this region.
View Article and Find Full Text PDFArch Microbiol
September 2025
Department of Infectious Disease, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, No. 639, Zhizaoju Road, Huangpu District, Shanghai, 200011, China.
Highly pathogenic avian influenza (HPAI) H5N1 virus poses a continuing global public health threat due to its outbreaks in poultry farms and zoonotic transmission from birds to humans. In the quest of effective therapeutics against H5N1 infection, antibodies with broad neutralizing activity have attracted significant attention. In this study, we employed a phage display technique to select and identify VHH antibodies with specific neutralizing activity against H5N1 hemagglutinin (HA) from an immune llama-derived antibody library.
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