Uniform poly(ethylene glycol) (PEG) oligomers, with a degree of polymerization n=1-40, were separated by preparative supercritical fluid chromatography from commercial monodispersed samples. Diffusion coefficients, D, for separated uniform PEG oligomers were measured in dilute solutions of deuterium oxide (D(2)O) at 30 degrees C, using pulsed-field gradient nuclear magnetic resonance. The measured D for each molecular weight was extrapolated to infinite dilution. Diffusion coefficients obtained at infinite dilution follow the scaling behavior of Zimm-type diffusion, even in the lower molecular weight range. Molecular-dynamics simulations for PEG in H(2)O also showed this scaling behavior, and reproduced close hydrodynamic interactions between PEG and water. These findings suggest that diffusion of PEG in water is dominated by hydrodynamic interaction over a wide molecular weight range, including at low molecular weights around 1000.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1063/1.1948378 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Extraction and Purification, Synthesis, Structure-activity Relationships, Pharmacological Effects and Mechanisms of Phillyrin: A Review.
Chem Biodivers
January 2025
Shaanxi University of Chinese Medicine, school of pharmacry, shiji Ave., 712046, xianyang, CHINA.
Phillyrin (PHI) is one of the main active components in Forsythia suspensa (Thunb.) Vahl, belonging to the class of lignans, which has anti-inflammatory, antioxidant, anti-tumor, antiviral, antibacterial, weight loss and other pharmacological effects, involving a variety of potential signaling pathways, such as TLR, NF-κB, PI3K/AKT, NRF2, PPAPs signaling pathways. The review search systematically and comprehensively CNKI, Wanfang, PubMed, Web of Science and other databases, screened nearly 100 relevant literature in the past five years, and summarized and evaluated the information of PHI extraction and purification, pharmacological activity, potential mechanism and structure-activity relationship.
View Article and Find Full Text PDFCelecoxib Enhances Oxidative Muscle Fibre Formation and Improves Muscle Functions Through Prokr1 Activation in Mice.
J Cachexia Sarcopenia Muscle
February 2025
Department of International Agricultural Technology, Graduate School of International Agricultural Technology, Seoul National University, Seoul, Republic of Korea.
Background: Muscle diseases are serious challenges to human health. Prokineticin receptor 1 (PROKR1) has emerged as a potential target to improve muscle function through increasing oxidative muscle fibres, but there are no clinically applicable synthetic PROKR1 agonists.
Methods: Drugs with biological properties of prokineticin 2 (PK2) were discovered through connectivity map (CMap) analysis.
Pharmacological effects of osimertinib on a chicken chorioallantoic membrane xenograft model with the EGFR exon-19-deleted advanced NSCLC mutation.
FEBS Open Bio
January 2025
Department of Pharmacology-Physiology-Toxicology, Institute of Pharmaceutical and Biological Sciences of Lyon, University Claude Bernard Lyon 1, France.
Non-small cell lung cancer (NSCLC) affects 10-50% of patients with epidermal growth factor receptor (EGFR) mutations. Osimertinib is a third-generation EGFR tyrosine kinase inhibitor (TKI) that radically changes the outcome of patients with tumors bearing EGFR sensitizing or EGFR T790M resistance mutations. However, resistance usually occurs, and new therapeutic combinations need to be explored.
View Article and Find Full Text PDFOptimization of Structure-guided Development of Chemical Probes for the Pseudoknot RNA of the Frameshift Element in SARS-CoV-2.
Angew Chem Int Ed Engl
January 2025
Goethe-Universitat Frankfurt am Main, Biochemistry, Chemistry, Pharmacy, GERMANY.
Targeting the RNA genome of SARS-CoV-2 is a viable option for antiviral drug development. We explored three ligand binding sites of the core pseudoknot RNA of the SARS-CoV-2 frameshift element. We iteratively optimized ligands, based on improved affinities, targeting these binding sites and report on structural and dynamic properties of the three identified binding sites.
View Article and Find Full Text PDFEffects of whey protein aggregates with different sizes on the gelatinization and retrogradation behavior of wheat starch.
J Sci Food Agric
January 2025
College of Food Science and Engineering, Northwest A&F University, Yangling, P. R. China.
Background: Starch retrogradation leads to undesirable changes in the texture and taste of starchy foods. The fibrous aggregates of whey protein fibrils (WPF) formed by heating under acidic conditions possess enhanced emulsification and foaming properties, but their effect on the retrogradation behavior of starch is unclear.
Results: WPFs with various molecular sizes were obtained by heating at 85 °C under acidic conditions (pH 2.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!