Matches in SemOpenAlex for { <https://semopenalex.org/work/W3149973335> ?p ?o ?g. }
- W3149973335 endingPage "3526" @default.
- W3149973335 startingPage "3510" @default.
- W3149973335 abstract "The aggregation of an intrinsically disordered protein, human islet amyloid polypeptide (hIAPP), leads to one of the most prevalent endocrine disorders, type II diabetes mellitus (T2DM). Hence inhibition of hIAPP aggregation provides a possible therapeutic approach for the treatment of T2DM. In this regard, a new aspect of adenosine triphosphate (ATP), which is widely known as the energy source for biological reactions, has recently been discovered, where it can inhibit the formation of protein aggregates and simultaneously dissolve preformed aggregates at a millimolar concentration scale. In this work, we investigate the effect of ATP on the aggregation of an amyloidogenic segment of hIAPP, hIAPP22–28, and also of the full length sequence. Using all-atom classical molecular dynamics simulations, we observe that the tendency of hIAPP to oligomerize into β-sheet conformers is inhibited by ATP, due to which the peptides remain distant, loosely packed random monomers. Moreover, it can also disassemble preformed hIAPP protofibrils. ATP preferentially interacts with the hydrophobic residues of hIAPP22–28 fragment and the terminal and turn residues of the full length peptide. The hydrogen bonding, hydrophobic, π–π, and N–H−π stacking interactions are the driving forces for the ATP induced inhibition of hIAPP aggregation. Interestingly, the hydrophobic adenosine of ATP is found to be more in contact with the peptide residues than the hydrophilic triphosphate moiety. The insight into the inhibitory mechanism of ATP on hIAPP aggregation can prove to be beneficial for the design of novel amyloid inhibitors in the future." @default.
- W3149973335 created "2021-04-13" @default.
- W3149973335 creator A5074940132 @default.
- W3149973335 creator A5080186508 @default.
- W3149973335 date "2021-04-01" @default.
- W3149973335 modified "2023-10-01" @default.
- W3149973335 title "Potential of ATP toward Prevention of hIAPP Oligomerization and Destabilization of hIAPP Protofibrils: An In Silico Perspective" @default.
- W3149973335 cites W1595575404 @default.
- W3149973335 cites W1768574001 @default.
- W3149973335 cites W1837066325 @default.
- W3149973335 cites W1964727310 @default.
- W3149973335 cites W1967820748 @default.
- W3149973335 cites W1969836007 @default.
- W3149973335 cites W1973897761 @default.
- W3149973335 cites W1974122968 @default.
- W3149973335 cites W1976499671 @default.
- W3149973335 cites W1979401635 @default.
- W3149973335 cites W1980035515 @default.
- W3149973335 cites W1980441015 @default.
- W3149973335 cites W1981225934 @default.
- W3149973335 cites W1981793913 @default.
- W3149973335 cites W1988583668 @default.
- W3149973335 cites W1993177346 @default.
- W3149973335 cites W2001629328 @default.
- W3149973335 cites W2003949305 @default.
- W3149973335 cites W2007236469 @default.
- W3149973335 cites W2008708467 @default.
- W3149973335 cites W2009788353 @default.
- W3149973335 cites W2016630460 @default.
- W3149973335 cites W2029667189 @default.
- W3149973335 cites W2035266068 @default.
- W3149973335 cites W2035687084 @default.
- W3149973335 cites W2036390519 @default.
- W3149973335 cites W2042822479 @default.
- W3149973335 cites W2044597283 @default.
- W3149973335 cites W2061111679 @default.
- W3149973335 cites W2061876586 @default.
- W3149973335 cites W2063464611 @default.
- W3149973335 cites W2063737568 @default.
- W3149973335 cites W2069110016 @default.
- W3149973335 cites W2069809597 @default.
- W3149973335 cites W2069858728 @default.
- W3149973335 cites W2070360911 @default.
- W3149973335 cites W2079000544 @default.
- W3149973335 cites W2080018640 @default.
- W3149973335 cites W2083164919 @default.
- W3149973335 cites W2084172070 @default.
- W3149973335 cites W2086295275 @default.
- W3149973335 cites W2088992037 @default.
- W3149973335 cites W2089361681 @default.
- W3149973335 cites W2105103540 @default.
- W3149973335 cites W2106140689 @default.
- W3149973335 cites W2109241488 @default.
- W3149973335 cites W2110175300 @default.
- W3149973335 cites W2112154906 @default.
- W3149973335 cites W2117537971 @default.
- W3149973335 cites W2121506107 @default.
- W3149973335 cites W2121779716 @default.
- W3149973335 cites W2124745408 @default.
- W3149973335 cites W2130308262 @default.
- W3149973335 cites W2132724034 @default.
- W3149973335 cites W2137204463 @default.
- W3149973335 cites W2147844096 @default.
- W3149973335 cites W2148828302 @default.
- W3149973335 cites W2160497181 @default.
- W3149973335 cites W2163421737 @default.
- W3149973335 cites W2165186407 @default.
- W3149973335 cites W2168978765 @default.
- W3149973335 cites W2175199342 @default.
- W3149973335 cites W2209022283 @default.
- W3149973335 cites W2218446246 @default.
- W3149973335 cites W2265775199 @default.
- W3149973335 cites W2271557333 @default.
- W3149973335 cites W2275283697 @default.
- W3149973335 cites W2300515376 @default.
- W3149973335 cites W2313719657 @default.
- W3149973335 cites W2315010380 @default.
- W3149973335 cites W2319252693 @default.
- W3149973335 cites W2329027920 @default.
- W3149973335 cites W2331980872 @default.
- W3149973335 cites W2332712348 @default.
- W3149973335 cites W2404280981 @default.
- W3149973335 cites W2412921526 @default.
- W3149973335 cites W2519877554 @default.
- W3149973335 cites W2540152008 @default.
- W3149973335 cites W2564509341 @default.
- W3149973335 cites W2568863654 @default.
- W3149973335 cites W2615607456 @default.
- W3149973335 cites W2750725325 @default.
- W3149973335 cites W2753315949 @default.
- W3149973335 cites W2769323464 @default.
- W3149973335 cites W2771682768 @default.
- W3149973335 cites W2788503048 @default.
- W3149973335 cites W2846468914 @default.
- W3149973335 cites W2883179995 @default.
- W3149973335 cites W2896637074 @default.
- W3149973335 cites W2900380335 @default.
- W3149973335 cites W2907093370 @default.