In search of selective inhibitors of cysteine protease, cathepsin K
(2005) In International Journal of Peptide Research and Therapeutics 11(3). p.203-209- Abstract
- Two potential azapeptide inhibitors of cathepsin K were designed and synthesized. To analyze in detail interactions between these azainhibitors and the investigated cysteine protease, molecular dynamics simulations were performed. For the obtained compounds the equilibrium constants for dissociation of inhibitor-enzyme complex, K-i, were determined. The examined azapeptides proved to be not as potent inhibitors of cathepsin K as they were expected to be according to the results of simulations. However, these calculations provide valuable information about probable structures of this type of peptidomimetics in the catalytic pocket of cathepsin K, which could be useful in designing of more selective inhibitors of this cysteine protease.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/224170
- author
- Wieczerzak, E ; Drabik, P ; Abrahamson, Magnus LU and Grubb, Anders LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- cysteine protease, azapeptide, cathepsin K, inhibitor, dynamics, molecular
- in
- International Journal of Peptide Research and Therapeutics
- volume
- 11
- issue
- 3
- pages
- 203 - 209
- publisher
- Springer
- external identifiers
-
- wos:000231889700004
- scopus:24044434903
- ISSN
- 1573-3904
- DOI
- 10.1007/s10989-005-6791-3
- language
- English
- LU publication?
- yes
- id
- a6167c2b-5f34-4b2f-881d-87d9ebb01372 (old id 224170)
- date added to LUP
- 2016-04-01 11:52:54
- date last changed
- 2023-01-03 00:44:02
@article{a6167c2b-5f34-4b2f-881d-87d9ebb01372, abstract = {{Two potential azapeptide inhibitors of cathepsin K were designed and synthesized. To analyze in detail interactions between these azainhibitors and the investigated cysteine protease, molecular dynamics simulations were performed. For the obtained compounds the equilibrium constants for dissociation of inhibitor-enzyme complex, K-i, were determined. The examined azapeptides proved to be not as potent inhibitors of cathepsin K as they were expected to be according to the results of simulations. However, these calculations provide valuable information about probable structures of this type of peptidomimetics in the catalytic pocket of cathepsin K, which could be useful in designing of more selective inhibitors of this cysteine protease.}}, author = {{Wieczerzak, E and Drabik, P and Abrahamson, Magnus and Grubb, Anders}}, issn = {{1573-3904}}, keywords = {{cysteine protease; azapeptide; cathepsin K; inhibitor; dynamics; molecular}}, language = {{eng}}, number = {{3}}, pages = {{203--209}}, publisher = {{Springer}}, series = {{International Journal of Peptide Research and Therapeutics}}, title = {{In search of selective inhibitors of cysteine protease, cathepsin K}}, url = {{http://dx.doi.org/10.1007/s10989-005-6791-3}}, doi = {{10.1007/s10989-005-6791-3}}, volume = {{11}}, year = {{2005}}, }