دورية أكاديمية
Interactions of poly(amidoamine) dendrimers with human serum albumin: binding constants and mechanisms.
| العنوان: | Interactions of poly(amidoamine) dendrimers with human serum albumin: binding constants and mechanisms. |
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| المؤلفون: | Giri J; Materials and Process Simulation Center, Division of Chemistry and Chemical Engineering, California Institute of Technology, USA., Diallo MS, Simpson AJ, Liu Y, Goddard WA, Kumar R, Woods GC |
| المصدر: | ACS nano [ACS Nano] 2011 May 24; Vol. 5 (5), pp. 3456-68. Date of Electronic Publication: 2011 Apr 01. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101313589 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1936-086X (Electronic) Linking ISSN: 19360851 NLM ISO Abbreviation: ACS Nano Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington D.C. : American Chemical Society |
| مواضيع طبية MeSH: | Dendrimers/*chemistry , Serum Albumin/*chemistry, Binding Sites ; Materials Testing ; Protein Binding |
| مستخلص: | The interactions of nanomaterials with plasma proteins have a significant impact on their in vivo transport and fate in biological fluids. This article discusses the binding of human serum albumin (HSA) to poly(amidoamine) [PAMAM] dendrimers. We use protein-coated silica particles to measure the HSA binding constants (K(b)) of a homologous series of 19 PAMAM dendrimers in aqueous solutions at physiological pH (7.4) as a function of dendrimer generation, terminal group, and core chemistry. To gain insight into the mechanisms of HSA binding to PAMAM dendrimers, we combined (1)H NMR, saturation transfer difference (STD) NMR, and NMR diffusion ordered spectroscopy (DOSY) of dendrimer-HSA complexes with atomistic molecular dynamics (MD) simulations of dendrimer conformation in aqueous solutions. The binding measurements show that the HSA binding constants (K(b)) of PAMAM dendrimers depend on dendrimer size and terminal group chemistry. The NMR (1)H and DOSY experiments indicate that the interactions between HSA and PAMAM dendrimers are relatively weak. The (1)H NMR STD experiments and MD simulations suggest that the inner shell protons of the dendrimers groups interact more strongly with HSA proteins. These interactions, which are consistently observed for different dendrimer generations (G0-NH(2)vs G4-NH(2)) and terminal groups (G4-NH(2)vs G4-OH with amidoethanol groups), suggest that PAMAM dendrimers adopt backfolded configurations as they form weak complexes with HSA proteins in aqueous solutions at physiological pH (7.4). |
| المشرفين على المادة: | 0 (Dendrimers) 0 (PAMAM Starburst) 0 (Serum Albumin) |
| تواريخ الأحداث: | Date Created: 20110329 Date Completed: 20110926 Latest Revision: 20110524 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1021/nn1021007 |
| PMID: | 21438566 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1936-086X |
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| DOI: | 10.1021/nn1021007 |