Journal
JOURNAL OF MOLECULAR GRAPHICS & MODELLING
Volume 110, Issue -, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jmgm.2021.108055
Keywords
TTR; EGCG; DMD; Aggregation; FEL; Resveratrol
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The study investigates the subversive nature of point mutation in TTR promoting amyloidogenicity using DMD simulations, and suggests the potential of resveratrol in mitigating the pathogenic repercussions of mutant TTR as an aid towards structure-based drug design in the research on familial amyloid disorders.
Transthyretin (TTR) mediated amyloidosis is a highly ruinous illness that affects various organs by aggravating the deposition of misfolded or mutated TTR protein aggregates in tissues. Hence, hindering the formation of TTR amyloid aggregates could be a key strategy in finding an effective cure towards the aggravating disorder. In this analysis, we examined the subversive nature of point mutation, V30M, in TTR that promotes amyloidogenicity using discrete molecular dynamics (DMD) simulations. Besides, we probed the association of naturally occurring polyphenols: EGCG (a proven anti TTR aggregation agent as positive control), resveratrol and curcumin in mitigating the pathogenic repercussions of mutant TTR. Results from the computational studies endorsed that the resveratrol constitutes a restorative potential to subjugate TTR mediated amyloidosis, besides EGCG. Hence, this study could be a reminiscent aspect in understanding the inhibitory role of key polyphenols against the mutant TTR aggregates, which could be an aid towards structure-based drug design in the upcoming research era on familial amyloid disorders.
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