SAR by NMR: Putting the Pieces Together

by: Philip J Hajduk

Mol. Interv., Vol. 6, No. 5. (1 October 2006), pp. 266-272.

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摘要

It has been nearly ten years since the introduction of SAR by NMR and the advent of fragment-based drug design. During this time, we have gained a tremendous amount of knowledge about protein druggability, the limits of chemical diversity, and crafting high-affinity ligands from low molecular weight, weakly binding leads. This review will describe the concept of fragment-based drug design, discuss why it works, and illustrate the power of the approach with two case studies on the design of potent inhibitors of matrix metalloproteinases and Bcl-2 family proteins. 10.1124/mi.6.5.8

@article{citeulike:1522930, abstract = {It has been nearly ten years since the introduction of SAR by NMR and the advent of fragment-based drug design. During this time, we have gained a tremendous amount of knowledge about protein druggability, the limits of chemical diversity, and crafting high-affinity ligands from low molecular weight, weakly binding leads. This review will describe the concept of fragment-based drug design, discuss why it works, and illustrate the power of the approach with two case studies on the design of potent inhibitors of matrix metalloproteinases and Bcl-2 family proteins. 10.1124/mi.6.5.8}, author = {Hajduk, Philip J. }, citeulike-article-id = {1522930}, doi = {http://dx.doi.org/10.1124/mi.6.5.8}, journal = {Mol. Interv.}, keywords = {nmr, sar}, month = {October}, number = {5}, pages = {266--272}, posted-at = {2007-07-30 20:23:59}, priority = {2}, title = {SAR by NMR: Putting the Pieces Together}, url = {http://dx.doi.org/10.1124/mi.6.5.8}, volume = {6}, year = {2006} }

RIS record

TY - JOUR ID - citeulike:1522930 L3 - citeulike-article-id:1522930 N2 - It has been nearly ten years since the introduction of SAR by NMR and the advent of fragment-based drug design. During this time, we have gained a tremendous amount of knowledge about protein druggability, the limits of chemical diversity, and crafting high-affinity ligands from low molecular weight, weakly binding leads. This review will describe the concept of fragment-based drug design, discuss why it works, and illustrate the power of the approach with two case studies on the design of potent inhibitors of matrix metalloproteinases and Bcl-2 family proteins. 10.1124/mi.6.5.8 IS - 5 JF - Mol. Interv. EP - 272 TI - SAR by NMR: Putting the Pieces Together VL - 6 SP - 266 KW - nmr KW - sar AU - Hajduk, Philip PY - 2006/10/01/ UR - http://dx.doi.org/10.1124/mi.6.5.8 ER -

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