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The present review covers proteomics discoveries in farm animals using combinatorial peptide ligand libraries (CPLLs). These libraries enhance the identification of low-abundance proteins by compressing the dynamic range of the protein concentration. This technology can be applied in multiple biological fluids, such as plasma or serum, follicular and cerebrospinal fluids, urine, saliva, tears seminal fluid, milk whey and even lymph. The discovery of low-abundance proteins contributes to the continuous monitoring for animal pathologies, which allows early treatment and disease prevention. Additionally, evidencing rare proteins in animal products used for human consumption can help in assessing their nutritional properties and their positive or negative effects on human health. SIGNIFICANCE: Many investigations are made on the identification of proteins of farm animals. Protein concentration changes under abnormal stressful conditions as a sign of a first physiological reaction. Many of these protein changes are of low-abundance and their detection is dependent on enrichment technologies. These changes are potentially correlated with the type of stressor and may determine actions to preserve the animal welfare.
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http://dx.doi.org/10.1016/j.jprot.2019.02.005 | DOI Listing |
Cell Rep
September 2025
State Key Laboratory of Pathogen and Biosecurity, Academy of Military Medical Sciences, Beijing 100071, China. Electronic address:
De novo design of antimicrobial peptides (AMPs) is challenging due to the vast combinatorial space and unknown mechanisms. We propose EBAMP, a generative-discriminative framework for de novo broad-spectrum AMP design targeting bacteria and fungi. EBAMP combines a Transformer-based generative model with advanced feature-based screening to explore peptide space and select multiobjective candidates.
View Article and Find Full Text PDFNat Commun
August 2025
Aix Marseille Univ, CNRS, Inserm, Institut Paoli-Calmettes, Centre de Recherche en Cancérologie de Marseille (CRCM), Marseille, France.
Histone deacetylases (HDACs) are epigenetic regulators frequently altered in cancer. Here we report that overexpression of HDAC1/2 occurs in Hepatocellular Carcinoma (HCC) patients, correlating with poor prognosis. We show that romidepsin, a class-I HDAC inhibitor, elicits a combinatorial perturbation of distinct molecular processes in HCC cells, altering lipid composition, mitotic spindle machinery, and levels of cell cycle/survival signals.
View Article and Find Full Text PDFMolecules
August 2025
iBB-Institute for Bioengineering and Biosciences, and Associate Laboratory i4HB-Institute for Health and Bioeconomy at Instituto Superior Técnico, Universidade de Lisboa, Av. Rovisco Pais, 1049-001 Lisboa, Portugal.
Plasmid DNA (pDNA) purification plays a key role in the development of vaccines and gene therapies. Affinity chromatography stands out as a promising method for plasmid purification, leveraging a range of biological and synthetic ligands to achieve selectivity. This study investigates the potential of a synthetic ligand library consisting of triazine-based bifunctional compounds designed to mimic the side chains of amino acids that are known to bind nucleic acids.
View Article and Find Full Text PDFBiomolecules
August 2025
School of Biosciences, College of Health and Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
The SpyTag-SpyCatcher system, developed by the Howarth lab, is based on splitting the CnaB2 domain from Streptococcus pyogenes into two parts: a 13-amino-acid SpyTag and a 116-amino-acid SpyCatcher. Upon incubation, they spontaneously form a covalent isopeptide bond between Asp7 (SpyTag) and Lys31 (SpyCatcher). This study explores whether the interaction specificity can be modulated by altering hydrophobic residues within the SpyCatcher binding pocket and corresponding SpyTag positions, potentially to create orthogonal SpyTag-SpyCatcher pairs.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
September 2025
Institute of Neuroscience, Technical University of Munich, Munich 80802, Germany.
Amyloid β (Aβ)-dependent circuit dysfunction in Alzheimer's disease (AD) is determined by a puzzling mix of hyperactive and inactive ("silent") brain neurons. Recent studies identified excessive glutamate accumulation as a key Aβ-dependent determinant of hyperactivity. The cellular mechanisms underlying neuronal silence depend on both Aβ and tau protein pathologies, with an unknown role of Aβ.
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