Document Detail


Understanding the Binding Interactions between Dendrimer and 18 Common Amino Acids by NMR Techniques.
MedLine Citation:
PMID:  21932783     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
In the present study, we focus on the interactions between poly(propylene imine) (PPI) dendrimer and eighteen of the twenty common amino acids by several NMR techniques including NMR titrations and NOESY analysis. Surface ionic interactions and interior encapsulations were observed and the binding behavior of amino acids with PPI dendrimer depends much on the side-chain properties of the amino acid, such as charge and hydrophobic/hydrophilic properties. The 1H NMR titration results show that the formation of PPI dendrimer-amino acid complexes are mainly driven by ionic interactions for all the amino acids except tryptophan, which is involved in strong hydrophobic interactions with the interior pockets of PPI. The hydrophobic encapsulation of tryptophan in PPI pockets is confirmed by NOESY analysis. Amino acids with negatively charged residues much more easily saturate the surface charges on PPI than amino acids with uncharged residues, while amino acids with positively charged residues are the most difficult to bind the surface amine groups on PPI dendrimer. A simultaneous occurrence of interior encapsulation (hydrophobic, hydrogen-bond, or ionic interactions) and surface binding (ionic interactions) was observed for tryptophan, phenylalanine, arginine, lysine, histidine, cysteine, and asparagine, and a preferential surface ionic binding on PPI surface rather than encapsulations in the interior was obtained for other amino acids.
Authors:
Mingming Wang; Yiyun Cheng; Xiaoliang Gong; Yihua Yu; Qun Chen; Jingjing Hu
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-9-20
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  -     ISSN:  1520-5207     ISO Abbreviation:  -     Publication Date:  2011 Sep 
Date Detail:
Created Date:  2011-9-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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