FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2008084426> ?p ?o ?g. }

• W2008084426 endingPage "217" @default.
• W2008084426 startingPage "189" @default.
• W2008084426 abstract "Pepstatin A, a pentapeptide with the molecular weight of 686, is a naturally occurring inhibitor of aspartyl proteasessecreted by Streptomyces species. Above a critical concentration of 0.1 mm at low ionic strength and neutral pH, it can polymerize into filaments which may extend over several micrometers. After negative staining, these filaments show a helical substructure with characteristic diameters ranging from 6 to 12 nm. Selected images at higher magnification suggest the filaments are composed of two intertwined 6 nm strands. This is in agreement with the optical diffraction analysis which additionally established a periodic pitch of 25 nm for the helical intertwining. Rotary shadowing of the pepstatin A filaments clearly demonstrated the right-handedness of the helical twist. In physiological salt solution or at higher concentrations of pepstatin A, a variety of higher order structures were observed, including ribbons, sheets and cylinders with both regular and twisted or irregular geometries. Pepstatin A can interact with intermediate filament subunit proteins. These proteins posses a long, α-helical rod domain that forms coiled-coil dimers, which through both hydrophobic and ionic interactions form tetramers which, in turn, in the presence of physiological salt concentrations, polymerize into the 10 nm intermediate filaments. In the absence of salt, pepstatin A and intermediate filament proteins polymerize into long filaments with a rough surface and a diameter of 15–17 nm. This polymerization appears to be primarily driven by nonionic interactions between pepstatin A and polymerization-competent forms of intermediate filament proteins, resulting in a composite filament. Polymerization-incompetent proteolytic fragments of vimentin, lacking portions of the head and/or tail domain, failed to copolymerize with pepstatin A into long filaments under these conditions. These peptides, as well as bovine serum albumin, were found to stick to the surface of pepstatin A filaments, ribbons and sheets. Independent evidence for direct association of pepstatin A with intermediate filament subunit proteins was provided not only by electron microscopy but also by UV difference spectra. Pepstatin A loses its ability to inhibit the aspartyl protease of the human immunodeficiency virus type 1 following polymerization into the higher order structures described here. The amazing fact that pepstatin A can spontaneously self-associate to form very large polymers seems to be a more rare event for such small peptides. The other examples of synthetic or naturally occurring oligopeptides discussed in this review which are able to polymerize into higher order structures possess a common property, their hydrophobicity, often manifested by clusters of valine or isoleucine residues. The mechanism of homo- or heteropolymerization may be of interest not only for model studies on the polymerization of small peptides, but also for practical development of soluble protease inhibitors and for the elucidation of the origin of the amyloid plaques of Alzheimer's disease and Down's syndrome, to name a few examples." @default.
• W2008084426 created "2016-06-24" @default.
• W2008084426 creator A5055081612 @default.
• W2008084426 creator A5085842763 @default.
• W2008084426 creator A5089203723 @default.
• W2008084426 date "1994-04-01" @default.
• W2008084426 modified "2023-09-25" @default.
• W2008084426 title "Pepstatin A: Polymerization of an oligopeptide" @default.
• W2008084426 cites W1041087405 @default.
• W2008084426 cites W1535278981 @default.
• W2008084426 cites W1619895170 @default.
• W2008084426 cites W1637218542 @default.
• W2008084426 cites W1775749144 @default.
• W2008084426 cites W1945883686 @default.
• W2008084426 cites W1955630041 @default.
• W2008084426 cites W1963659992 @default.
• W2008084426 cites W1964125059 @default.
• W2008084426 cites W1967279802 @default.
• W2008084426 cites W1968996863 @default.
• W2008084426 cites W1970661613 @default.
• W2008084426 cites W1976820443 @default.
• W2008084426 cites W1977976545 @default.
• W2008084426 cites W1982695192 @default.
• W2008084426 cites W1984623612 @default.
• W2008084426 cites W1984711953 @default.
• W2008084426 cites W1987057827 @default.
• W2008084426 cites W1990149590 @default.
• W2008084426 cites W1991489244 @default.
• W2008084426 cites W1995135104 @default.
• W2008084426 cites W1998084493 @default.
• W2008084426 cites W1999123457 @default.
• W2008084426 cites W2001768218 @default.
• W2008084426 cites W2003434690 @default.
• W2008084426 cites W2008524154 @default.
• W2008084426 cites W2015105601 @default.
• W2008084426 cites W2017643275 @default.
• W2008084426 cites W2017880839 @default.
• W2008084426 cites W2020975457 @default.
• W2008084426 cites W2021417643 @default.
• W2008084426 cites W2023519337 @default.
• W2008084426 cites W2024423815 @default.
• W2008084426 cites W2026410708 @default.
• W2008084426 cites W2028453323 @default.
• W2008084426 cites W2030808787 @default.
• W2008084426 cites W2032920422 @default.
• W2008084426 cites W2040779333 @default.
• W2008084426 cites W2055765332 @default.
• W2008084426 cites W2056046302 @default.
• W2008084426 cites W2057395131 @default.
• W2008084426 cites W2059062385 @default.
• W2008084426 cites W2059433846 @default.
• W2008084426 cites W2059457068 @default.
• W2008084426 cites W2067462759 @default.
• W2008084426 cites W2077896437 @default.
• W2008084426 cites W2079990598 @default.
• W2008084426 cites W2081881251 @default.
• W2008084426 cites W2087202090 @default.
• W2008084426 cites W2091505182 @default.
• W2008084426 cites W2114661152 @default.
• W2008084426 cites W2119297613 @default.
• W2008084426 cites W2123011045 @default.
• W2008084426 cites W2320852204 @default.
• W2008084426 cites W2338449952 @default.
• W2008084426 cites W2397874191 @default.
• W2008084426 cites W4239594472 @default.
• W2008084426 cites W2022266441 @default.
• W2008084426 doi "https://doi.org/10.1016/0968-4328(94)90042-6" @default.
• W2008084426 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8055247" @default.
• W2008084426 hasPublicationYear "1994" @default.
• W2008084426 type Work @default.
• W2008084426 sameAs 2008084426 @default.
• W2008084426 citedByCount "6" @default.
• W2008084426 countsByYear W20080844262020 @default.
• W2008084426 crossrefType "journal-article" @default.
• W2008084426 hasAuthorship W2008084426A5055081612 @default.
• W2008084426 hasAuthorship W2008084426A5085842763 @default.
• W2008084426 hasAuthorship W2008084426A5089203723 @default.
• W2008084426 hasConcept C12554922 @default.
• W2008084426 hasConcept C14228908 @default.
• W2008084426 hasConcept C142669718 @default.
• W2008084426 hasConcept C1491633281 @default.
• W2008084426 hasConcept C178790620 @default.
• W2008084426 hasConcept C181199279 @default.
• W2008084426 hasConcept C185592680 @default.
• W2008084426 hasConcept C188027245 @default.
• W2008084426 hasConcept C192562407 @default.
• W2008084426 hasConcept C2776350231 @default.
• W2008084426 hasConcept C2776714187 @default.
• W2008084426 hasConcept C44228677 @default.
• W2008084426 hasConcept C521977710 @default.
• W2008084426 hasConcept C55493867 @default.
• W2008084426 hasConcept C78383274 @default.
• W2008084426 hasConcept C8010536 @default.
• W2008084426 hasConcept C86803240 @default.
• W2008084426 hasConceptScore W2008084426C12554922 @default.
• W2008084426 hasConceptScore W2008084426C14228908 @default.
• W2008084426 hasConceptScore W2008084426C142669718 @default.
• W2008084426 hasConceptScore W2008084426C1491633281 @default.

• next