Design of protease inhibitors
There is a general parallelism in the strategy followed in the design of hormonal peptide analogs and protease inhibitors. However, in the latter, one more dimension has been added with the development of mechanism‐based inhibitors, a dimension that is not yet available for hormonal peptides because...
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| Veröffentlicht in: | Biopolymers 1981-09, Vol.20 (9), p.2001-2010 |
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| container_end_page | 2010 |
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| container_issue | 9 |
| container_start_page | 2001 |
| container_title | Biopolymers |
| container_volume | 20 |
| creator | Ondetti, M. A. Cushman, D. W. |
| description | There is a general parallelism in the strategy followed in the design of hormonal peptide analogs and protease inhibitors. However, in the latter, one more dimension has been added with the development of mechanism‐based inhibitors, a dimension that is not yet available for hormonal peptides because of the lack of knowledge about receptor mechanisms. The recently advanced concepts of transition state and bi‐product analogs have made possible the development of highly potent active‐site directed reversible protease inhibitors of great therapeutic potential. |
| doi_str_mv | 10.1002/bip.1981.360200922 |
| format | Article |
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The recently advanced concepts of transition state and bi‐product analogs have made possible the development of highly potent active‐site directed reversible protease inhibitors of great therapeutic potential.</description><subject>Amino Acid Sequence</subject><subject>Angiotensin-Converting Enzyme Inhibitors</subject><subject>Animals</subject><subject>hormones</subject><subject>inhibitors</subject><subject>peptide synthesis</subject><subject>peptides</subject><subject>Protease Inhibitors - chemical synthesis</subject><subject>proteinase</subject><subject>Structure-Activity Relationship</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtKw0AUhgdRaq2-gFDoyl3qmUtmMuBGW1sLxQsogpthkp7oaNrUmRTt25uSUtzp6iz-C__5CDml0KcA7Dx1yz7VCe1zCQxAM7ZH2hS0ioAlbJ-0AUBGPGbxITkK4R1ACE6hRVqSKaYB2qQ7xOBeF70y7y19WaEN2HOLN5e6qvThmBzktgh4sr0d8jS6fhzcRNO78WRwOY0ywYBFSqf1HA6KU4o8t9JqxbIkYRQxBS4wtUppGmurudVCWknB8iynoGaZTGe8Q86a3nrD5wpDZeYuZFgUdoHlKhjFFU8gTv400liASGJdG1ljzHwZgsfcLL2bW782FMwGnqnhmQ08s4NXh7rb9lU6x9kusqVV6xeN_uUKXP-j0VxN7n_XR03chQq_d3HrP4ysP4zN8-3YvIynYjh6UIbzH2p8iF0</recordid><startdate>198109</startdate><enddate>198109</enddate><creator>Ondetti, M. 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| fulltext | fulltext |
| identifier | ISSN: 0006-3525 |
| ispartof | Biopolymers, 1981-09, Vol.20 (9), p.2001-2010 |
| issn | 0006-3525 1097-0282 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73738058 |
| source | MEDLINE; Wiley Online Library All Journals |
| subjects | Amino Acid Sequence Angiotensin-Converting Enzyme Inhibitors Animals hormones inhibitors peptide synthesis peptides Protease Inhibitors - chemical synthesis proteinase Structure-Activity Relationship |
| title | Design of protease inhibitors |
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