Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/5234
Title: | Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin | Authors: | Shnyrov, Valery L. Villar, Enrique Zhadan, Galina G. Sanchez-Ruiz, Jose M. Quintas, Alexandre Saraiva, Maria João M. Brito, Rui M. M. |
Keywords: | Transthyretin; Familial amyloidotic polyneuropathy; Differential scanning calorimetry; Thermal stability | Issue Date: | 2000 | Citation: | Biophysical Chemistry. 88:1-3 (2000) 61-67 | Abstract: | Familial amyloidotic polyneuropathy (FAP) is an autosomal dominant hereditary type of amyloidosis involving amino acid substitutions in transthyretin (TTR). V30M-TTR is the most frequent variant, and L55P-TTR is the variant associated with the most aggressive form of FAP. The thermal stability of the wild-type, V30M-TTR, L55P-TTR and a non-amyloidogenic variant, T119M-TTR, was studied by high-sensitivity differential scanning calorimetry (DSC). The thermal unfolding of TTR is a spontaneous reversible process involving a highly co-operative transition between folded tetramers and unfolded monomers. All variants of transthyretin are very stable to the thermal unfolding that occurs at very high temperatures, most probably because of their oligomeric structure. The data presented in this work indicated that for the homotetrameric form of the wild-type TTR and its variants, the order of stability is as follows: wild-type TTRT119M-TTR>L55P-TTR>V30M-TTR, which does not correlate with their known amyloidogenic potential. | URI: | https://hdl.handle.net/10316/5234 | DOI: | 10.1016/S0301-4622(00)00199-X | Rights: | openAccess |
Appears in Collections: | FCTUC Química - Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
file4b15859df382481ca650920faecb7d28.pdf | 175.9 kB | Adobe PDF | View/Open |
SCOPUSTM
Citations
54
checked on Oct 14, 2024
WEB OF SCIENCETM
Citations
47
checked on Oct 2, 2024
Page view(s) 50
429
checked on Oct 15, 2024
Download(s)
407
checked on Oct 15, 2024
Google ScholarTM
Check
Altmetric
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.