FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2151216250> ?p ?o ?g. }

• W2151216250 endingPage "3045" @default.
• W2151216250 startingPage "3039" @default.
• W2151216250 abstract "The synthetic lipid-associating peptide, LAP-20 (VSSLLSSLKEYWSSLKESFS), activates lecithin-cholesterol acyltransferase (LCAT) despite its lack of sequence homology to apolipoprotein A-I, the primary in vivo activator of LCAT. Using SDS and dodecylphosphocholine (DPC) to model the lipoprotein environment, the structural features responsible for LAP-20's ability to activate LCAT were studied by optical and two-dimensional 1H NMR spectroscopy. A large blue shift in the intrinsic fluorescence of LAP-20 with the addition of detergent suggested that the peptide formed a complex with the micelles. Analysis of the CD data shows that LAP-20 lacks well defined structure in aqueous solution but adopts helical, ordered conformations upon the addition of SDS or DPC. The helical nature of the peptides in the presence of both lipids was confirmed by upfield Hα NMR secondary shifts relative to random coil values. Average structures for both peptides in aqueous solutions containing SDS and DPC were generated using distance geometry methods from 329 (SDS) and 309 (DPC) nuclear Overhauser effect-based distance restraints. The backbone (N, Cα, C=O) RMSD from the average structure of an ensemble of 17 out of 20 calculated structures was 0.41 ± 0.15 Å for LAP-20 in SDS and 0.41 ± 0.12 Å for an ensemble of 20 out of 20 calculated structures for LAP-20 in DPC. In the presence of SDS, the distance geometry and simulated annealing calculations show that LAP-20 adopts a well defined class A amphipathic helix with distinct hydrophobic and hydrophilic faces. A similar structure was obtained for LAP-20 in the presence of DPC, suggesting that both detergents may be used interchangeably to model the lipoprotein environment. Conformational features of the calculated structures for LAP-20 are discussed relative to models for apolipoprotein A-I activation of LCAT. The synthetic lipid-associating peptide, LAP-20 (VSSLLSSLKEYWSSLKESFS), activates lecithin-cholesterol acyltransferase (LCAT) despite its lack of sequence homology to apolipoprotein A-I, the primary in vivo activator of LCAT. Using SDS and dodecylphosphocholine (DPC) to model the lipoprotein environment, the structural features responsible for LAP-20's ability to activate LCAT were studied by optical and two-dimensional 1H NMR spectroscopy. A large blue shift in the intrinsic fluorescence of LAP-20 with the addition of detergent suggested that the peptide formed a complex with the micelles. Analysis of the CD data shows that LAP-20 lacks well defined structure in aqueous solution but adopts helical, ordered conformations upon the addition of SDS or DPC. The helical nature of the peptides in the presence of both lipids was confirmed by upfield Hα NMR secondary shifts relative to random coil values. Average structures for both peptides in aqueous solutions containing SDS and DPC were generated using distance geometry methods from 329 (SDS) and 309 (DPC) nuclear Overhauser effect-based distance restraints. The backbone (N, Cα, C=O) RMSD from the average structure of an ensemble of 17 out of 20 calculated structures was 0.41 ± 0.15 Å for LAP-20 in SDS and 0.41 ± 0.12 Å for an ensemble of 20 out of 20 calculated structures for LAP-20 in DPC. In the presence of SDS, the distance geometry and simulated annealing calculations show that LAP-20 adopts a well defined class A amphipathic helix with distinct hydrophobic and hydrophilic faces. A similar structure was obtained for LAP-20 in the presence of DPC, suggesting that both detergents may be used interchangeably to model the lipoprotein environment. Conformational features of the calculated structures for LAP-20 are discussed relative to models for apolipoprotein A-I activation of LCAT." @default.
• W2151216250 created "2016-06-24" @default.
• W2151216250 creator A5029635607 @default.
• W2151216250 creator A5033465444 @default.
• W2151216250 creator A5047614339 @default.
• W2151216250 creator A5071438010 @default.
• W2151216250 creator A5078167253 @default.
• W2151216250 date "1996-02-01" @default.
• W2151216250 modified "2023-09-30" @default.
• W2151216250 title "Structural Studies of a Peptide Activator of Human Lecithin-Cholesterol Acyltransferase" @default.
• W2151216250 cites W1504017858 @default.
• W2151216250 cites W1522544439 @default.
• W2151216250 cites W1540308607 @default.
• W2151216250 cites W1541852335 @default.
• W2151216250 cites W1573404455 @default.
• W2151216250 cites W1576149482 @default.
• W2151216250 cites W1584791707 @default.
• W2151216250 cites W1635128112 @default.
• W2151216250 cites W1947043095 @default.
• W2151216250 cites W1969333714 @default.
• W2151216250 cites W1971251199 @default.
• W2151216250 cites W1971966571 @default.
• W2151216250 cites W1972459558 @default.
• W2151216250 cites W1976684587 @default.
• W2151216250 cites W1983113757 @default.
• W2151216250 cites W1985796903 @default.
• W2151216250 cites W1990328005 @default.
• W2151216250 cites W1993844842 @default.
• W2151216250 cites W1994967652 @default.
• W2151216250 cites W1997354900 @default.
• W2151216250 cites W2006925909 @default.
• W2151216250 cites W2007237294 @default.
• W2151216250 cites W2009148109 @default.
• W2151216250 cites W2013005355 @default.
• W2151216250 cites W2019178773 @default.
• W2151216250 cites W2020745281 @default.
• W2151216250 cites W2024803155 @default.
• W2151216250 cites W2027912460 @default.
• W2151216250 cites W2033299688 @default.
• W2151216250 cites W2037692676 @default.
• W2151216250 cites W2038214413 @default.
• W2151216250 cites W2039587858 @default.
• W2151216250 cites W2045950270 @default.
• W2151216250 cites W2064517997 @default.
• W2151216250 cites W2074539156 @default.
• W2151216250 cites W2074770586 @default.
• W2151216250 cites W2075954862 @default.
• W2151216250 cites W2076530860 @default.
• W2151216250 cites W2076921684 @default.
• W2151216250 cites W2085213735 @default.
• W2151216250 cites W2088615805 @default.
• W2151216250 cites W2108890051 @default.
• W2151216250 cites W2111149713 @default.
• W2151216250 cites W2114471659 @default.
• W2151216250 cites W2123916335 @default.
• W2151216250 cites W2126521510 @default.
• W2151216250 cites W2139266365 @default.
• W2151216250 cites W2172093339 @default.
• W2151216250 cites W2334261900 @default.
• W2151216250 cites W2341638556 @default.
• W2151216250 cites W2401829918 @default.
• W2151216250 cites W2442172771 @default.
• W2151216250 cites W35241519 @default.
• W2151216250 doi "https://doi.org/10.1074/jbc.271.6.3039" @default.
• W2151216250 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8621698" @default.
• W2151216250 hasPublicationYear "1996" @default.
• W2151216250 type Work @default.
• W2151216250 sameAs 2151216250 @default.
• W2151216250 citedByCount "21" @default.
• W2151216250 countsByYear W21512162502022 @default.
• W2151216250 crossrefType "journal-article" @default.
• W2151216250 hasAuthorship W2151216250A5029635607 @default.
• W2151216250 hasAuthorship W2151216250A5033465444 @default.
• W2151216250 hasAuthorship W2151216250A5047614339 @default.
• W2151216250 hasAuthorship W2151216250A5071438010 @default.
• W2151216250 hasAuthorship W2151216250A5078167253 @default.
• W2151216250 hasBestOaLocation W21512162501 @default.
• W2151216250 hasConcept C11268172 @default.
• W2151216250 hasConcept C12554922 @default.
• W2151216250 hasConcept C133571119 @default.
• W2151216250 hasConcept C178790620 @default.
• W2151216250 hasConcept C184651966 @default.
• W2151216250 hasConcept C185592680 @default.
• W2151216250 hasConcept C2779281246 @default.
• W2151216250 hasConcept C2779564620 @default.
• W2151216250 hasConcept C34349673 @default.
• W2151216250 hasConcept C55493867 @default.
• W2151216250 hasConcept C62614982 @default.
• W2151216250 hasConcept C71240020 @default.
• W2151216250 hasConcept C8010536 @default.
• W2151216250 hasConcept C86803240 @default.
• W2151216250 hasConceptScore W2151216250C11268172 @default.
• W2151216250 hasConceptScore W2151216250C12554922 @default.
• W2151216250 hasConceptScore W2151216250C133571119 @default.
• W2151216250 hasConceptScore W2151216250C178790620 @default.
• W2151216250 hasConceptScore W2151216250C184651966 @default.
• W2151216250 hasConceptScore W2151216250C185592680 @default.
• W2151216250 hasConceptScore W2151216250C2779281246 @default.

• next