دورية أكاديمية
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Protein Binding Leads to Reduced Stability and Solvated Disorder in the Polystyrene Nanoparticle Corona.

التفاصيل البيبلوغرافية
العنوان: Protein Binding Leads to Reduced Stability and Solvated Disorder in the Polystyrene Nanoparticle Corona.
المؤلفون: Somarathne RP; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA., Amarasekara DL; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA., Kariyawasam CS; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA., Robertson HA; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA., Mayatt R; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA., Gwaltney SR; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA., Fitzkee NC; Department of Chemistry, Mississippi State University, Mississippi State, MS, 39762, USA.
المصدر: Small (Weinheim an der Bergstrasse, Germany) [Small] 2024 Jun; Vol. 20 (26), pp. e2305684. Date of Electronic Publication: 2024 Jan 21.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Wiley-VCH Country of Publication: Germany NLM ID: 101235338 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1613-6829 (Electronic) Linking ISSN: 16136810 NLM ISO Abbreviation: Small Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Weinheim, Germany : Wiley-VCH, c2005-
مواضيع طبية MeSH: Polystyrenes*/chemistry , Nanoparticles*/chemistry , Protein Binding* , Protein Corona*/chemistry, Solvents/chemistry ; Hydrophobic and Hydrophilic Interactions ; Particle Size
مستخلص: Understanding the conformation of proteins in the nanoparticle corona has important implications in how organisms respond to nanoparticle-based drugs. These proteins coat the nanoparticle surface, and their properties will influence the nanoparticle's interaction with cell targets and the immune system. While some coronas are thought to be disordered, two key unanswered questions are the degree of disorder and solvent accessibility. Here, a model is developed for protein corona disorder in polystyrene nanoparticles of varying size. For two different proteins, it is found that binding affinity decreases as nanoparticle size increases. The stoichiometry of binding, along with changes in the hydrodynamic size, supports a highly solvated, disordered protein corona anchored at a small number of attachment sites. The scaling of the stoichiometry versus nanoparticle size is consistent with disordered polymer dimensions. Moreover, it is found that proteins are destabilized less in the presence of larger nanoparticles, and hydrophobic exposure decreases at lower curvatures. The observations hold for proteins on flat polystyrene surfaces, which have the lowest hydrophobic exposure. The model provides an explanation for previous observations of increased amyloid fibrillation rates in the presence of larger nanoparticles, and it may rationalize how cell receptors can recognize protein disorder in therapeutic nanoparticles.
(© 2024 Wiley‐VCH GmbH.)
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معلومات مُعتمدة: R01 AI139479 United States AI NIAID NIH HHS; 1818090 National Science Foundation; R01AI139479 National Institute of Allergy and Infectious Diseases of the National Institutes of Health
فهرسة مساهمة: Keywords: interactions; nanoparticle; protein corona; structure
المشرفين على المادة: 0 (Polystyrenes)
0 (Protein Corona)
0 (Solvents)
تواريخ الأحداث: Date Created: 20240122 Date Completed: 20240626 Latest Revision: 20240628
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC11209821
DOI: 10.1002/smll.202305684
PMID: 38247186
قاعدة البيانات: MEDLINE
الوصف
تدمد:1613-6829
DOI:10.1002/smll.202305684