Title : Temperature dependence of Congo red binding to amyloid β12-28.

Pub. Date : 2013 Jun

PMID : 23636660






14 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Because Congo red (CR) can bind to critical intermediate structural forms of amyloid beta (Abeta), it has been suggested as a potential therapeutic agent against neurodegenerative disorders such as Alzheimer"s disease. Congo Red amyloid beta precursor protein Homo sapiens
2 Because Congo red (CR) can bind to critical intermediate structural forms of amyloid beta (Abeta), it has been suggested as a potential therapeutic agent against neurodegenerative disorders such as Alzheimer"s disease. Congo Red amyloid beta precursor protein Homo sapiens
3 Because Congo red (CR) can bind to critical intermediate structural forms of amyloid beta (Abeta), it has been suggested as a potential therapeutic agent against neurodegenerative disorders such as Alzheimer"s disease. Congo Red amyloid beta precursor protein Homo sapiens
4 Because Congo red (CR) can bind to critical intermediate structural forms of amyloid beta (Abeta), it has been suggested as a potential therapeutic agent against neurodegenerative disorders such as Alzheimer"s disease. Congo Red amyloid beta precursor protein Homo sapiens
5 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
6 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
7 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
8 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
9 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
10 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
11 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
12 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
13 Studies conducted between 15 and 35 C show that binding of CR to Abeta(12-28) was strongly dependent on temperature, with a decrease in CR-Abeta(12-28) complexation as temperature increases, presumably because of conformational changes within Abeta(12-28) at the highest temperatures, that conceal the CR binding sites. Congo Red amyloid beta precursor protein Homo sapiens
14 In fact, no CR binding was observed at 35 C. The binding of CR to Abeta(12-28) was associated with favorable changes in both enthalpy and entropy that resulted in binding constants (K) of between 10(5) and 10(6) M (-1). Congo Red amyloid beta precursor protein Homo sapiens