Switch-Peptides: From Conformational Studies to Alzheimer's Disease
Studies on designed peptides that exhibit high tendencies for medium-induced conformational transitions have recently attracted much attention because structural changes are considered as molecular key processes in degenerative diseases. The experimental access to these events has been lim...
| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | deu |
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Swiss Chemical Society
2006-04-01
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| Series: | CHIMIA |
| Subjects: | |
| Online Access: | https://chimia.ch/chimia/article/view/4147 |
| _version_ | 1798014448165715968 |
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| author | Lydiane Saucède Gabriele Tuchscherer Hilal Lashuel John Lopez Jacques Dubochet Marc Adrian Eric Grouzmann Jérémy Bérard Marie-Stéphanie Camus Karine Murat Richard Mimna Bhubaneswar Mandal Arunan Chandravarkar Sonia Dos Santos Manfred Mutter |
| author_facet | Lydiane Saucède Gabriele Tuchscherer Hilal Lashuel John Lopez Jacques Dubochet Marc Adrian Eric Grouzmann Jérémy Bérard Marie-Stéphanie Camus Karine Murat Richard Mimna Bhubaneswar Mandal Arunan Chandravarkar Sonia Dos Santos Manfred Mutter |
| author_sort | Lydiane Saucède |
| collection | DOAJ |
| description |
Studies on designed peptides that exhibit high tendencies for medium-induced conformational transitions have recently attracted much attention because structural changes are considered as molecular key processes in degenerative diseases. The experimental access to these events has been
limited so far mainly due to the intrinsic tendency of the involved polypeptides for self-association and aggregation, e.g. amyloid ? plaque formation, thought to be at the origin of Alzheimer's disease. We have developed a new concept termed 'switch-peptides' which allows the
controlled onset of polypeptide folding and misfolding in vitro and in vivo, starting from a soluble, non-toxic precursor molecule. As a major feature, the folding process is initiated by enzyme-triggered N,O-acyl migrations restoring the native peptide backbone in situ.
As the folding is set off in the moment of creating the bioactive molecule ('in statu nascendi', ISN), our concept allows for the first time the investigation of the early steps of protein misfolding as relevant in degenerative diseases, opening new perspectives for the rational design
of therapeutically relevant compounds.
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| first_indexed | 2024-04-11T15:17:31Z |
| format | Article |
| id | doaj.art-beccaf2ffee6472d961290e3338aea85 |
| institution | Directory Open Access Journal |
| issn | 0009-4293 2673-2424 |
| language | deu |
| last_indexed | 2024-04-11T15:17:31Z |
| publishDate | 2006-04-01 |
| publisher | Swiss Chemical Society |
| record_format | Article |
| series | CHIMIA |
| spelling | doaj.art-beccaf2ffee6472d961290e3338aea852022-12-22T04:16:27ZdeuSwiss Chemical SocietyCHIMIA0009-42932673-24242006-04-0160410.2533/000942906777674921Switch-Peptides: From Conformational Studies to Alzheimer's DiseaseLydiane SaucèdeGabriele TuchschererHilal LashuelJohn LopezJacques DubochetMarc AdrianEric GrouzmannJérémy BérardMarie-Stéphanie CamusKarine MuratRichard MimnaBhubaneswar MandalArunan ChandravarkarSonia Dos SantosManfred Mutter Studies on designed peptides that exhibit high tendencies for medium-induced conformational transitions have recently attracted much attention because structural changes are considered as molecular key processes in degenerative diseases. The experimental access to these events has been limited so far mainly due to the intrinsic tendency of the involved polypeptides for self-association and aggregation, e.g. amyloid ? plaque formation, thought to be at the origin of Alzheimer's disease. We have developed a new concept termed 'switch-peptides' which allows the controlled onset of polypeptide folding and misfolding in vitro and in vivo, starting from a soluble, non-toxic precursor molecule. As a major feature, the folding process is initiated by enzyme-triggered N,O-acyl migrations restoring the native peptide backbone in situ. As the folding is set off in the moment of creating the bioactive molecule ('in statu nascendi', ISN), our concept allows for the first time the investigation of the early steps of protein misfolding as relevant in degenerative diseases, opening new perspectives for the rational design of therapeutically relevant compounds. https://chimia.ch/chimia/article/view/4147Degenerative diseasesInduction of biological functionProtein misfoldingRational drug designSwitch-peptides |
| spellingShingle | Lydiane Saucède Gabriele Tuchscherer Hilal Lashuel John Lopez Jacques Dubochet Marc Adrian Eric Grouzmann Jérémy Bérard Marie-Stéphanie Camus Karine Murat Richard Mimna Bhubaneswar Mandal Arunan Chandravarkar Sonia Dos Santos Manfred Mutter Switch-Peptides: From Conformational Studies to Alzheimer's Disease CHIMIA Degenerative diseases Induction of biological function Protein misfolding Rational drug design Switch-peptides |
| title | Switch-Peptides: From Conformational Studies to Alzheimer's Disease |
| title_full | Switch-Peptides: From Conformational Studies to Alzheimer's Disease |
| title_fullStr | Switch-Peptides: From Conformational Studies to Alzheimer's Disease |
| title_full_unstemmed | Switch-Peptides: From Conformational Studies to Alzheimer's Disease |
| title_short | Switch-Peptides: From Conformational Studies to Alzheimer's Disease |
| title_sort | switch peptides from conformational studies to alzheimer s disease |
| topic | Degenerative diseases Induction of biological function Protein misfolding Rational drug design Switch-peptides |
| url | https://chimia.ch/chimia/article/view/4147 |
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