کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10591806 | 981761 | 2014 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Protein-ligand interactions: Probing the energetics of a putative cation-Ï interaction
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Protein-ligand interactions: Probing the energetics of a putative cation-Ï interaction Protein-ligand interactions: Probing the energetics of a putative cation-Ï interaction](/preview/png/10591806.png)
چکیده انگلیسی
In order to probe the energetics associated with a putative cation-Ï interaction, thermodynamic parameters are determined for complex formation between the Grb2 SH2 domain and tripeptide derivatives of RCO-pTyr-Ac6c-Asn wherein the R group is varied to include different alkyl, cycloalkyl, and aryl groups. Although an indole ring is reputed to have the strongest interaction with a guanidinium ion, binding free energies, ÎG°, for derivatives of RCO-pTyr-Ac6c-Asn bearing cyclohexyl and phenyl groups were slightly more favorable than their indolyl analog. Crystallographic analysis of two complexes reveals that test ligands bind in similar poses with the notable exception of the relative orientation and proximity of the phenyl and indolyl rings relative to an arginine residue of the domain. These spatial orientations are consistent with those observed in other cation-Ï interactions, but there is no net energetic benefit to such an interaction in this biological system. Accordingly, although cation-Ï interactions are well documented as important noncovalent forces in molecular recognition, the energetics of such interactions may be mitigated by other nonbonded interactions and solvation effects in protein-ligand associations.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 24, Issue 14, 15 July 2014, Pages 3164-3167
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 24, Issue 14, 15 July 2014, Pages 3164-3167
نویسندگان
James M. Myslinski, John H. Clements, Stephen F. Martin,