Difference between revisions of "Part:BBa K4165160"
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Tau binding peptide targeting the PHF seed of Tau | Tau binding peptide targeting the PHF seed of Tau | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | + | Arginine (R) is a basic amino acid with the presence of a guanidino group at its aliphatic side chain. It is typically protonated at physiological pH where the guanidino group turns into a cationic guanidinium moiety that is highly stable and able to self-associate and cluster. These properties contribute to the intra- and intermolecular associations of arginine residues, as it provides a great capacity for electrostatic interactions (especially hydrogen-bonding) that results in a tendency to form stable clusters in solution. | |
| − | <span class='h3bb'>Sequence and Features</span> | + | |
| + | Arginine has long been recognized as a chemical chaperone, with its ability to interact with and influence proteins in solution. In silico experiments have proved its ability to bind protein surfaces for a long time through its carboxyl and guanidinium groups, and form clusters through self-association with other arginine molecules. This has led to various in vitro experiments that proved the ability of arginine to suppress protein aggregations, which made it a very interesting candidate in the modulation of proteopathies correlated with Alzheimer’s disease like tau and amyloid beta aggregations. | ||
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| + | <span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span> | ||
<partinfo>BBa_K4165160 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165160 SequenceAndFeatures</partinfo> | ||
Latest revision as of 15:07, 11 October 2022
R32
Tau binding peptide targeting the PHF seed of Tau
Usage and Biology
Arginine (R) is a basic amino acid with the presence of a guanidino group at its aliphatic side chain. It is typically protonated at physiological pH where the guanidino group turns into a cationic guanidinium moiety that is highly stable and able to self-associate and cluster. These properties contribute to the intra- and intermolecular associations of arginine residues, as it provides a great capacity for electrostatic interactions (especially hydrogen-bonding) that results in a tendency to form stable clusters in solution.
Arginine has long been recognized as a chemical chaperone, with its ability to interact with and influence proteins in solution. In silico experiments have proved its ability to bind protein surfaces for a long time through its carboxyl and guanidinium groups, and form clusters through self-association with other arginine molecules. This has led to various in vitro experiments that proved the ability of arginine to suppress protein aggregations, which made it a very interesting candidate in the modulation of proteopathies correlated with Alzheimer’s disease like tau and amyloid beta aggregations.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]