NDLI: Models for the binding channel of wild type and mutant transthyretin with glabridin

Content Provider	Royal Society of Chemistry (RSC)
Author	Zhu, Jingxuan Zou, Liyun Han, Weiwei Guo, Yingjie Dong, Yang Zhou, Hui
Copyright Year	2016
Abstract	Transthyretin (TTR) is a protein whose aggregation and deposition can lead to human amyloid diseases. V30A TTR is a TTR variant observed in some familial amyloidotic polyneuropathy (FAP) patients. Here we report that V30A TTR exhibits a significantly lower glabridin (Glab) binding energy than exhibited by wild-type TTR (WT TTR) in vitro. To compare changes in structural conformation induced by Glab binding to WT TTR and the V30A mutant, molecular dynamics (MD) simulations were used. Our results indicate that additional high-occupancy hydrogen bonds were observed at the binding interface between the two dimers in V30A TTR, while stabilisation hydrophobic interactions between residues in the mutant AB loop decreased. These results suggest that AC and BD contacts between the two dimers are positioned closer together in the mutant. Our results should provide useful clues to guide future TTR studies.
Starting Page	96816
Ending Page	96823
Page Count	8
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	6
Issue Number	99
Journal	RSC Advances
DOI	10.1039/c6ra19814g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Glabridin Binding energy Glab Transthyretin Molecular dynamics Hydrophobic effect Amyloid Mutation Conformational change Protein Hydrogen bond
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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