FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2753608750> ?p ?o ?g. }

• W2753608750 abstract "Protein aggregation occurs under many circumstances, from the dynamic assembly of tubulin to form microtubules, the aggregation of actin into filaments, as well as plaque formation by amyloid precipitation. One important requirement in studying the mechanism of amyloid aggregation is the ability to monitor the growth kinetics over a wide range in size scales (10 nm to microns) with time that spans microseconds to seconds. Understanding the mechanisms of the aggregation may then lead to improved design of drugs to help control or suppress the aggregation process. In this dissertation, the physical characterization of the â-amyloid peptide and its interaction with áá-amino acid peptide-based mediators was investigated from the early, rapidly evolving stage to the later, slowly diffusing peptide stage by the application of fluorescence photobleaching recovery (FPR). The diffusion rates of â-amyloid peptide and â-amyloid assemblies under the effects of variables including concentration of â-amyloid, blocker peptide, ionic strength, pH, time and temperature were accessible by this method. In some instances, dynamic light scattering (DLS), which acquire signals greater than 10 decades of lag times, without requiring a dye label was used for comparison and to account for the limitations of any given approach. Attachment of 5-carboxyfluorescein did not affect the integrity of the protein and the measured diffusion coefficients were similar to those measured by diffusion ordered spectroscopy (DOSY) and from theoretical expectations. FPR proved more sensitive than DLS for detection of low oligomer aggregates of the â-amyloid peptide coexisting with much larger fibrils. We were able to reverse the conformation of the peptide from the low oligomeric state to the aggregated state under neutral and acidic pH conditions and confirmed that the peptide growth increased with increasing ionic strength. The interaction of â-amyloid peptide with membranes results in several membrane-perturbing effects which may play a pivotal role in the pathogenic cascade leading to Alzheimer’s disease. Model phospholipid bilayer membranes consisting of 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-Phosphocholine (POPC) and 1-Oleoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino] dodecanoyl]-sn-Glycero-3-Phosphocholine (18:1-12:0 NBD PC) were prepared on mica. FPR proved to be a useful technique for obtaining information of the nature of membrane fluidity upon interaction with the â-amyloid peptide." @default.
• W2753608750 created "2017-09-15" @default.
• W2753608750 creator A5044362051 @default.
• W2753608750 date "2022-06-10" @default.
• W2753608750 modified "2023-10-15" @default.
• W2753608750 title "Characterization of Beta-amyloid Peptide Aggregation and Acceleration with Non-fibrillar Forming Peptide-based Mediators" @default.
• W2753608750 cites W1515644524 @default.
• W2753608750 cites W1574528366 @default.
• W2753608750 cites W1606860533 @default.
• W2753608750 cites W1771027239 @default.
• W2753608750 cites W1964563386 @default.
• W2753608750 cites W1964592445 @default.
• W2753608750 cites W1965839087 @default.
• W2753608750 cites W1967549235 @default.
• W2753608750 cites W1968324562 @default.
• W2753608750 cites W1968906927 @default.
• W2753608750 cites W1969073916 @default.
• W2753608750 cites W1969272199 @default.
• W2753608750 cites W1970808851 @default.
• W2753608750 cites W1973134139 @default.
• W2753608750 cites W1973203775 @default.
• W2753608750 cites W1974137193 @default.
• W2753608750 cites W1976820443 @default.
• W2753608750 cites W1977182743 @default.
• W2753608750 cites W1982033147 @default.
• W2753608750 cites W1982635793 @default.
• W2753608750 cites W1982685650 @default.
• W2753608750 cites W1991655565 @default.
• W2753608750 cites W1992004763 @default.
• W2753608750 cites W1994928619 @default.
• W2753608750 cites W1998429632 @default.
• W2753608750 cites W1998592142 @default.
• W2753608750 cites W2000769077 @default.
• W2753608750 cites W2015675204 @default.
• W2753608750 cites W2016243005 @default.
• W2753608750 cites W2017643275 @default.
• W2753608750 cites W2019369720 @default.
• W2753608750 cites W2026277335 @default.
• W2753608750 cites W2029526541 @default.
• W2753608750 cites W2032131088 @default.
• W2753608750 cites W2039112917 @default.
• W2753608750 cites W2041443037 @default.
• W2753608750 cites W2042408115 @default.
• W2753608750 cites W2044897724 @default.
• W2753608750 cites W2045664839 @default.
• W2753608750 cites W2045777307 @default.
• W2753608750 cites W2047046753 @default.
• W2753608750 cites W2047863709 @default.
• W2753608750 cites W2048779945 @default.
• W2753608750 cites W2049535318 @default.
• W2753608750 cites W2054086227 @default.
• W2753608750 cites W2055485145 @default.
• W2753608750 cites W2056692194 @default.
• W2753608750 cites W2060085692 @default.
• W2753608750 cites W2064578334 @default.
• W2753608750 cites W2065802357 @default.
• W2753608750 cites W2070887142 @default.
• W2753608750 cites W2071953900 @default.
• W2753608750 cites W2076166680 @default.
• W2753608750 cites W2076834744 @default.
• W2753608750 cites W2081537428 @default.
• W2753608750 cites W2082698296 @default.
• W2753608750 cites W2082790072 @default.
• W2753608750 cites W2089843826 @default.
• W2753608750 cites W2096410114 @default.
• W2753608750 cites W2096601751 @default.
• W2753608750 cites W2099077346 @default.
• W2753608750 cites W2121753059 @default.
• W2753608750 cites W2123321976 @default.
• W2753608750 cites W2127265740 @default.
• W2753608750 cites W2145904082 @default.
• W2753608750 cites W2154589026 @default.
• W2753608750 cites W2158482458 @default.
• W2753608750 cites W2168102821 @default.
• W2753608750 cites W2950027825 @default.
• W2753608750 cites W3130044479 @default.
• W2753608750 cites W2952867034 @default.
• W2753608750 doi "https://doi.org/10.31390/gradschool_dissertations.3212" @default.
• W2753608750 hasPublicationYear "2022" @default.
• W2753608750 type Work @default.
• W2753608750 sameAs 2753608750 @default.
• W2753608750 citedByCount "0" @default.
• W2753608750 crossrefType "dissertation" @default.
• W2753608750 hasAuthorship W2753608750A5044362051 @default.
• W2753608750 hasBestOaLocation W27536087501 @default.
• W2753608750 hasConcept C121332964 @default.
• W2753608750 hasConcept C12554922 @default.
• W2753608750 hasConcept C1276947 @default.
• W2753608750 hasConcept C134018914 @default.
• W2753608750 hasConcept C136238340 @default.
• W2753608750 hasConcept C142724271 @default.
• W2753608750 hasConcept C144618238 @default.
• W2753608750 hasConcept C14631669 @default.
• W2753608750 hasConcept C147789679 @default.
• W2753608750 hasConcept C148898269 @default.
• W2753608750 hasConcept C155672457 @default.
• W2753608750 hasConcept C165220095 @default.
• W2753608750 hasConcept C171250308 @default.
• W2753608750 hasConcept C178790620 @default.
• W2753608750 hasConcept C179104552 @default.

• next