The future of lactoferrin: A closer look at LipoDuo technology.

Background: Lactoferrin (Lf), a multifunctional glycoprotein known for its roles in immune modulation, iron metabolism, and antimicrobial activity, has limited therapeutic efficacy due to poor bioavailability. Liposomal encapsulation of lactoferrin (LLf) offers a potential solution by improving its stability, absorption, and sustained release, making it a promising candidate for various clinical applications. This study aims to compare the effectiveness of LLf and plain Lf in cellular uptake, proliferation, and wound healing using HEK-293T and Caco-2 cell lines.

Comparative investigation of lung adenocarcinoma and squamous cell carcinoma transcriptome to reveal potential candidate biomarkers: An explainable AI approach.

Patients with Non-Small Cell Lung Cancer (NSCLC) present a variety of clinical symptoms, such as dyspnea and chest pain, complicating accurate diagnosis. NSCLC includes subtypes distinguished by histological characteristics, specifically lung adenocarcinoma (LUAD) and lung squamous cell carcinoma (LUSC). This study aims to compare and identify abnormal gene expression patterns in LUAD and LUSC samples relative to adjacent healthy tissues using an explainable artificial intelligence (XAI) framework.

Epidermal Growth Factor Receptors Unveiled: A Comprehensive Survey on Mutations, Clinical Insights of Global Inhibitors, and Emergence of Heterocyclic Derivatives as EGFR Inhibitors.

Mutations that overexpress the epidermal growth factor receptor (EGFR) are linked to cancers like breast (15-20%), head and neck (10-15%), colorectal (5-8%), and non-small cell lung cancer (10-50%), especially in East Asian populations. EGFR activation stimulates "RAS/RAF/MEK/ERK, PI3K/Akt, and MAPK" pathways, which enhance cell division, survival, angiogenesis, and tumor growth while inhibiting apoptosis and metastasis. Secondary mutations (e.

Conformational dynamics of the membrane protein of MERS-CoV in comparison with SARS-CoV-2 in ERGIC complex.

The present study explores the conformational dynamics of the membrane protein of Middle East Respiratory Syndrome Coronavirus (MERS-CoV) within the Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) complex using an all-atomistic molecular dynamics simulation approach. Significant structural changes were observed in the N-terminal, C-terminal, transmembrane, and beta-sheet sandwich domains of the MERS-CoV membrane protein. This study also highlights the structural similarities between the MERS-CoV and the SARS-CoV-2 membrane proteins, particularly in how both exhibit a distinct kink in the transmembrane helix caused by aromatic residue-lipid interactions.