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• W4386725508 endingPage "8175" @default.
• W4386725508 startingPage "8162" @default.
• W4386725508 abstract "α-amyloids present a novel self-assembly principle that can be utilized to prepare functional biomaterials. Evidence of α-amyloid formation in the active core of the human LL-37 protein (comprising residues 17 to 29) was associated with this peptide's membranolytic property. Though mechanistic pathways of β-amyloid formation are known, such studies are scarce in α-amyloids. Modern computational techniques allow such mechanistic studies in molecular detail. Here, we propose aggregation pathways in hLL-3717-29 through molecular dynamics simulations. We first identified oligomers among peptides based on a distance criterion. The distribution of oligomers was then used to build Markov state models from which pathways were obtained using the framework of transition path theory. We checked the structural stability of the peptides during oligomerization, which is crucial from their functional point of view. We also investigated the key residues that participate in oligomer formation, the interactions between them, and the effect of residue mutations on the binding free energy of the peptides. Our findings suggest that larger oligomers are produced from the association of smaller and intermediate oligomers. The peptides retain their helical structure during aggregation with transient occurrences of 3-10 helix and turns. Hydrophobic interactions are vital in the aggregation of these peptides with Ile24 playing a crucial role. Mutation of this residue to alanine decreases the peptides' binding free energy, resulting in reduced aggregation tendency." @default.
• W4386725508 created "2023-09-15" @default.
• W4386725508 creator A5018368886 @default.
• W4386725508 creator A5080186508 @default.
• W4386725508 date "2023-09-14" @default.
• W4386725508 modified "2023-10-14" @default.
• W4386725508 title "Pathways of hLL-37_17-29 Aggregation Give Insight into the Mechanism of α-Amyloid Formation" @default.
• W4386725508 cites W1482266509 @default.
• W4386725508 cites W1536005838 @default.
• W4386725508 cites W1935356375 @default.
• W4386725508 cites W1940255949 @default.
• W4386725508 cites W1966355489 @default.
• W4386725508 cites W1967069761 @default.
• W4386725508 cites W1967610865 @default.
• W4386725508 cites W1968721593 @default.
• W4386725508 cites W1968984443 @default.
• W4386725508 cites W1970577444 @default.
• W4386725508 cites W1971042231 @default.
• W4386725508 cites W1971948710 @default.
• W4386725508 cites W1976499671 @default.
• W4386725508 cites W1979070806 @default.
• W4386725508 cites W1981225934 @default.
• W4386725508 cites W1994321237 @default.
• W4386725508 cites W2003949305 @default.
• W4386725508 cites W2007593295 @default.
• W4386725508 cites W2020799333 @default.
• W4386725508 cites W2023826687 @default.
• W4386725508 cites W2031843459 @default.
• W4386725508 cites W2035266068 @default.
• W4386725508 cites W2035687084 @default.
• W4386725508 cites W2036135772 @default.
• W4386725508 cites W2043782614 @default.
• W4386725508 cites W2046285452 @default.
• W4386725508 cites W2047599457 @default.
• W4386725508 cites W2053348581 @default.
• W4386725508 cites W2053354380 @default.
• W4386725508 cites W2055484248 @default.
• W4386725508 cites W2057071131 @default.
• W4386725508 cites W2063116767 @default.
• W4386725508 cites W2064367582 @default.
• W4386725508 cites W2066795144 @default.
• W4386725508 cites W2075088552 @default.
• W4386725508 cites W2076253721 @default.
• W4386725508 cites W2083164919 @default.
• W4386725508 cites W2084878620 @default.
• W4386725508 cites W2085899859 @default.
• W4386725508 cites W2086368575 @default.
• W4386725508 cites W2093333472 @default.
• W4386725508 cites W2094036101 @default.
• W4386725508 cites W2096015012 @default.
• W4386725508 cites W2106140689 @default.
• W4386725508 cites W2109119409 @default.
• W4386725508 cites W2117537971 @default.
• W4386725508 cites W2118382442 @default.
• W4386725508 cites W2120569780 @default.
• W4386725508 cites W2127536099 @default.
• W4386725508 cites W2133709240 @default.
• W4386725508 cites W2137790756 @default.
• W4386725508 cites W2142868265 @default.
• W4386725508 cites W2144286887 @default.
• W4386725508 cites W2158323088 @default.
• W4386725508 cites W2162741488 @default.
• W4386725508 cites W2163210644 @default.
• W4386725508 cites W2164128280 @default.
• W4386725508 cites W2169759699 @default.
• W4386725508 cites W2212327748 @default.
• W4386725508 cites W2226825552 @default.
• W4386725508 cites W2265694288 @default.
• W4386725508 cites W2295272344 @default.
• W4386725508 cites W2313116527 @default.
• W4386725508 cites W2324140061 @default.
• W4386725508 cites W2327581403 @default.
• W4386725508 cites W2330799739 @default.
• W4386725508 cites W2332712348 @default.
• W4386725508 cites W2404280981 @default.
• W4386725508 cites W2416087370 @default.
• W4386725508 cites W2558558076 @default.
• W4386725508 cites W2619203867 @default.
• W4386725508 cites W2766262938 @default.
• W4386725508 cites W2768678455 @default.
• W4386725508 cites W2771230435 @default.
• W4386725508 cites W2794208617 @default.
• W4386725508 cites W2817784260 @default.
• W4386725508 cites W2915521488 @default.
• W4386725508 cites W2918255589 @default.
• W4386725508 cites W2922133433 @default.
• W4386725508 cites W2940314661 @default.
• W4386725508 cites W2997773874 @default.
• W4386725508 cites W3024001683 @default.
• W4386725508 cites W3047308476 @default.
• W4386725508 cites W3108599616 @default.
• W4386725508 cites W3120995461 @default.
• W4386725508 cites W4206431129 @default.
• W4386725508 cites W4206677002 @default.
• W4386725508 cites W4310639020 @default.
• W4386725508 cites W4315927538 @default.
• W4386725508 cites W4376224198 @default.
• W4386725508 doi "https://doi.org/10.1021/acs.jpcb.3c04742" @default.

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