Using combinatorial methods to arrive at a quantitative structure–stability relationship for a new class of one-armed cationic peptide receptors targeting the C-terminus of the amyloid β-peptideElectronic supplementary information (ESI) available: quantitative on bead binding assay. See http://www.rsc.org/suppdata/ob/b2/b211425a/

2003 ◽  
Vol 1 (4) ◽  
pp. 633-636 ◽  
Author(s):  
Carsten Schmuck ◽  
Martin Heil
Keyword(s):  
Binding Assay ◽  
Amyloid Β ◽  
Supplementary Information ◽  
Structure Stability ◽  
Quantitative Structure ◽  
Cationic Peptide ◽  
Peptide Receptors ◽  
New Class ◽  
C Terminus ◽  
Combinatorial Methods

The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites

2015 ◽  
Vol 192 (3) ◽  
pp. 336-341 ◽  
Author(s):  
Plínio Salmazo Vieira ◽  
Priscila Oliveira de Giuseppe ◽  
Arthur Henrique Cavalcante de Oliveira ◽  
Mario Tyago Murakami
Keyword(s):  
Quaternary Structure ◽  
Nucleoside Diphosphate Kinase ◽  
Structure Stability ◽  
C Terminus ◽  
Leishmania Parasites

scholarly journals New Class of Inhibitors of Amyloid-β Fibril Formation

2002 ◽  
Vol 277 (45) ◽  
pp. 42881-42890 ◽  
Author(s):  
Hilal A. Lashuel ◽  
Dean M. Hartley ◽  
David Balakhaneh ◽  
Aneel Aggarwal ◽  
Saul Teichberg ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Fibril Formation ◽  
New Class

scholarly journals Human Albumin Impairs Amyloid β-peptide Fibrillation Through its C-terminus: From docking Modeling to Protection Against Neurotoxicity in Alzheimer's disease

2019 ◽  
Vol 17 ◽  
pp. 963-971 ◽  
Author(s):  
Pol Picón-Pagès ◽  
Jaume Bonet ◽  
Javier García-García ◽  
Joan Garcia-Buendia ◽  
Daniela Gutierrez ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Β ◽  
Human Albumin ◽  
Amyloid Β Peptide ◽  
C Terminus

scholarly journals Copper(II)-induced self-oligomerization of α-synuclein

1999 ◽  
Vol 340 (3) ◽  
pp. 821-828 ◽  
Author(s):  
Seung R. PAIK ◽  
Hyun-Ju SHIN ◽  
Ju-Hyun LEE ◽  
Chung-Soon CHANG ◽  
Jongsun KIM
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Metal Ion ◽  
Senile Plaques ◽  
Lewy Bodies ◽  
Amyloid Β ◽  
Coupling Reagents ◽  
C Terminus ◽  
Nucleation Centre ◽  
The Common

α-Synuclein is a component of the abnormal protein depositions in senile plaques and Lewy bodies of Alzheimer's disease (AD) and Parkinson's disease respectively. The protein was suggested to provide a possible nucleation centre for plaque formation in AD via selective interaction with amyloid β/A4 protein (Aβ). We have shown previously that α-synuclein has experienced self-oligomerization when Aβ25-35 was present in an orientation-specific manner in the sequence. Here we examine this biochemically specific self-oligomerization with the use of various metals. Strikingly, copper(II) was the most effective metal ion affecting α-synuclein to form self-oligomers in the presence of coupling reagents such as dicyclohexylcarbodi-imide or N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline. The size distribution of the oligomers indicated that monomeric α-synuclein was oligomerized sequentially. The copper-induced oligomerization was shown to be suppressed as the acidic C-terminus of α-synuclein was truncated by treatment with endoproteinase Asp-N. In contrast, the Aβ25-35-induced oligomerizations of the intact and truncated forms of α-synuclein were not affected. This clearly indicated that the copper-induced oligomerization was dependent on the acidic C-terminal region and that its underlying biochemical mechanism was distinct from that of the Aβ25-35-induced oligomerization. Although the physiological or pathological relevance of the oligomerization remains currently elusive, the common outcome of α-synuclein on treatment with copper or Aβ25-35 might be useful in understanding neurodegenerative disorders in molecular terms. In addition, abnormal copper homoeostasis could be considered as one of the risk factors for the development of disorders such as AD or Parkinson's disease.

C-Terminal Analogues of Parathyroid Hormone:  Effect of C-Terminus Function on Helical Structure, Stability, and Bioactivity

Biochemistry ◽  
2006 ◽  
Vol 45 (37) ◽  
pp. 11113-11121 ◽  
Author(s):  
Zhanna Potetinova ◽  
Jean-René Barbier ◽  
Tanya Suen ◽  
Thomas Dean ◽  
Thomas J. Gardella ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Helical Structure ◽  
Structure Stability ◽  
C Terminus ◽  
Hormone Effect
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