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231225s2018 xx |||||o 00| ||eng c |
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7 |
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|a 10.1021/acs.langmuir.7b03617
|2 doi
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|a pubmed25n0931.xml
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|a (NLM)29284085
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Jha, Anjali
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Inhibition of β-Amyloid Aggregation through a Designed β-Hairpin Peptide
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| 264 |
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1 |
|c 2018
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 17.09.2018
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|a Date Revised 17.09.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Designing peptide-based drugs to target the β-sheet-rich toxic intermediates during the aggregation of amyloid-β 1-42 (Aβ1-42) has been a major challenge. In general, β-sheet breaker peptides (BSBPs) are designed to complement the enthalpic interactions with the aggregating protein, and entropic effects are usually ignored. Here, we have developed a conformationally constrained cyclic BSBP by the use of an unnatural amino acid and a disulfide bond. We show that our peptide strongly inhibits the aggregation of Aβ1-42 in a concentration-dependent manner. It stabilizes the random coil conformation of Aβ1-42 monomers and inhibits the secondary structural transition to a β-sheet-rich conformation which allows Aβ1-42 to oligomerize in an ordered assembly during its aggregation. Our cyclic peptide also rescues the toxicity of soluble aggregates of Aβ1-42 toward neuronal cells. However, it significantly loses its potency in the conformationally relaxed acyclic form. It appears that limiting the loss of conformational entropy of the BSBP ligand can play a very important role in the attainment of conformations for precise and tight binding, making them a potent inhibitor for Aβ1-42 amyloidosis
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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| 650 |
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|a Amyloid beta-Peptides
|2 NLM
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| 650 |
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7 |
|a Peptide Fragments
|2 NLM
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| 650 |
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|a Peptides
|2 NLM
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| 650 |
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|a Peptides, Cyclic
|2 NLM
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| 700 |
1 |
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|a Kumar, Mothukuri Ganesh
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Gopi, Hosahudya N
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Paknikar, Kishore M
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 34(2018), 4 vom: 30. Jan., Seite 1591-1600
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
8 |
|g volume:34
|g year:2018
|g number:4
|g day:30
|g month:01
|g pages:1591-1600
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| 856 |
4 |
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|u http://dx.doi.org/10.1021/acs.langmuir.7b03617
|3 Volltext
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|d 34
|j 2018
|e 4
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|h 1591-1600
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