Matches in SemOpenAlex for { <https://semopenalex.org/work/W4230038961> ?p ?o ?g. }
Showing items 1 to 70 of
70
with 100 items per page.
- W4230038961 endingPage "24" @default.
- W4230038961 startingPage "15" @default.
- W4230038961 abstract "There are a number of naturally occurring motifs for lipidation of peptides and proteins. In cases in which this involves adding a single hydrocarbon chain to the peptide, it is either a fatty acid or an isoprenyl group. Lipopeptides will partition between membrane and aqueous phases. When only one hydrocarbon chain is attached to the peptide, the affinity of the lipopeptide for the membrane is only marginally increased over that of the free peptide. The resulting partitioning is largely determined by the extent of the interaction of the peptide moiety with the membrane. In contrast, lipidation involving two hydrocarbon chains, either as two single chains attached at distinct locations of the peptide or a double-chain lipid anchor, firmly attaches the lipopeptide to the membrane. This can allow the placement of specific binding sites on a membrane surface. Such a strategy can be used, for example, to place specific antibodies on the surface of drug-carrying liposomes for the purpose of targeting drug delivery. In addition, lipopeptides will alter the physical properties of membranes. One of these effects is to increase the bilayer to hexagonal phase transition temperature. Substances having this property may also alter functional properties of membranes. While it is unlikely that these changes in the biophysical properties of the membrane are responsible for specific functions of lipopeptides, such changes may be used to modulate certain properties of a membrane, such as the rate of viral fusion. © 1997 John Wiley & Sons, Inc. Biopoly 43: 15–24, 1997" @default.
- W4230038961 created "2022-05-11" @default.
- W4230038961 creator A5054602401 @default.
- W4230038961 date "1997-01-01" @default.
- W4230038961 modified "2023-09-25" @default.
- W4230038961 title "Biophysical studies of lipopeptide‐membrane interactions" @default.
- W4230038961 doi "https://doi.org/10.1002/(sici)1097-0282(1997)43:1<15::aid-bip3>3.3.co;2-t" @default.
- W4230038961 hasPublicationYear "1997" @default.
- W4230038961 type Work @default.
- W4230038961 citedByCount "0" @default.
- W4230038961 crossrefType "journal-article" @default.
- W4230038961 hasAuthorship W4230038961A5054602401 @default.
- W4230038961 hasConcept C103038307 @default.
- W4230038961 hasConcept C125501631 @default.
- W4230038961 hasConcept C12554922 @default.
- W4230038961 hasConcept C185154212 @default.
- W4230038961 hasConcept C185592680 @default.
- W4230038961 hasConcept C190283241 @default.
- W4230038961 hasConcept C192157962 @default.
- W4230038961 hasConcept C193469717 @default.
- W4230038961 hasConcept C203522944 @default.
- W4230038961 hasConcept C21951064 @default.
- W4230038961 hasConcept C2777425210 @default.
- W4230038961 hasConcept C2779281246 @default.
- W4230038961 hasConcept C39944091 @default.
- W4230038961 hasConcept C41625074 @default.
- W4230038961 hasConcept C523546767 @default.
- W4230038961 hasConcept C54355233 @default.
- W4230038961 hasConcept C55493867 @default.
- W4230038961 hasConcept C71240020 @default.
- W4230038961 hasConcept C86803240 @default.
- W4230038961 hasConceptScore W4230038961C103038307 @default.
- W4230038961 hasConceptScore W4230038961C125501631 @default.
- W4230038961 hasConceptScore W4230038961C12554922 @default.
- W4230038961 hasConceptScore W4230038961C185154212 @default.
- W4230038961 hasConceptScore W4230038961C185592680 @default.
- W4230038961 hasConceptScore W4230038961C190283241 @default.
- W4230038961 hasConceptScore W4230038961C192157962 @default.
- W4230038961 hasConceptScore W4230038961C193469717 @default.
- W4230038961 hasConceptScore W4230038961C203522944 @default.
- W4230038961 hasConceptScore W4230038961C21951064 @default.
- W4230038961 hasConceptScore W4230038961C2777425210 @default.
- W4230038961 hasConceptScore W4230038961C2779281246 @default.
- W4230038961 hasConceptScore W4230038961C39944091 @default.
- W4230038961 hasConceptScore W4230038961C41625074 @default.
- W4230038961 hasConceptScore W4230038961C523546767 @default.
- W4230038961 hasConceptScore W4230038961C54355233 @default.
- W4230038961 hasConceptScore W4230038961C55493867 @default.
- W4230038961 hasConceptScore W4230038961C71240020 @default.
- W4230038961 hasConceptScore W4230038961C86803240 @default.
- W4230038961 hasIssue "1" @default.
- W4230038961 hasLocation W42300389611 @default.
- W4230038961 hasOpenAccess W4230038961 @default.
- W4230038961 hasPrimaryLocation W42300389611 @default.
- W4230038961 hasRelatedWork W2019176710 @default.
- W4230038961 hasRelatedWork W2033588568 @default.
- W4230038961 hasRelatedWork W2043051289 @default.
- W4230038961 hasRelatedWork W2065854005 @default.
- W4230038961 hasRelatedWork W2161536338 @default.
- W4230038961 hasRelatedWork W2419410760 @default.
- W4230038961 hasRelatedWork W2604676471 @default.
- W4230038961 hasRelatedWork W3011024476 @default.
- W4230038961 hasRelatedWork W4285389466 @default.
- W4230038961 hasRelatedWork W2340590315 @default.
- W4230038961 hasVolume "43" @default.
- W4230038961 isParatext "false" @default.
- W4230038961 isRetracted "false" @default.
- W4230038961 workType "article" @default.