52060-82-9Relevant articles and documents
Manganese catalysts with C1-symmetric N4 ligand for enantioselective epoxidation of olefins
Wang, Bin,Miao, Chengxia,Wang, Shoufeng,Xia, Chungu,Sun, Wei
supporting information; scheme or table, p. 6750 - 6753 (2012/07/03)
Bioinspired manganese complexes based on N4 ligands, with a more rigid, chiral diamine derived from proline and two benzimidazoles, were synthesized and applied to epoxidize olefins with hydrogen peroxide as a clean oxidant. Notably, 60-99 % isolated yields and excellent ee values (up to 95 %) were obtained by using low catalyst loadings (0.01-0.2 mol %; see scheme; F green, S yellow). Copyright
Compounds binding to the S2-S3 pockets of thrombin
Nilsson, Mikael,H?m?l?inen, Markku,Ivarsson, Maria,Gottfries, Johan,Xue, Yafeng,Hansson, Sebastian,Isaksson, Roland,Fex, Tomas
experimental part, p. 2708 - 2715 (2010/01/16)
A set of compounds designed to bind to the S2-S3 pockets of thrombin was prepared. These compounds included examples with no interactions in the S1 pocket. Proline, a common P2 in many thrombin inhibitors, was combined with known P3 residues and P1 substituents of varying size and lipophilicity. Binding constants were determined using surface plasmon resonance (SPR) biosensor technology and were found to be in good agreement with results from an enzyme assay. A dramatic increase in affinity (100-1000 times) was seen for compounds incorporating an amino group capable of forming a hydrogen bond with gly216 in the protein backbone. The ligand efficiency was increased by including substituents that form stronger hydrophobic interactions with the P1 pocket. The binding mode was confirmed by X-ray analysis, which revealed the anticipated binding motif that included hydrogen bonds as well as a tightly bound water molecule. A QSAR model indicated that hydrogen bonding and lipophilicity were important for the prediction of binding constants. The results described here may have implications for how directed compound libraries for shallow protein pockets, like S2 and S3 in serine proteases, can be designed.
Factors Affecting Conformation in Proline-Containing Peptides
Taylor, Carol M.,Hardre, Renaud,Edwards, Patrick J. B.,Park, Jae H.
, p. 4413 - 4416 (2007/10/03)
(Equation presented) NMR was used to study the thermodynamics of the cis → trans isomerization for prolyl amide bonds in the compounds shown. The magnitude of Kt/c for C-terminal esters is greater than for the corresponding amides, signifying s
