2011 Fiscal Year Final Research Report
Development of a novel amino acid solubility propensity scale for the calculation of polypeptide solubility
| Project/Area Number |
21300110
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Bioinformatics/Life informatics
|
|---|
| Research Institution | Tokyo University of Agriculture and Technology |
|---|
Principal Investigator |
KURODA Yutaka 東京農工大学, 大学院・工学研究院, 准教授 (10312240)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
TOH Hiroyuki 産業技術総合研究所, 生命情報工学研究センター, 副研究センター長 (70192656)
|
|---|
| Project Period (FY) |
2009 – 2011
|
| Keywords | タンパク質凝集 / 会合自由エネルギー / 溶解度測定 / 溶解度向上タグ / 熱力学 / 単純化タンパク質 / ホスト・ゲスト法 |
|---|
| Research Abstract |
Protein solubility is usually characterized in terms of a hydrophobicity scale, which refers to the free energy of transfer of a molecule from an aqueous to a nonpolar solution and is not a "solubility propensity scale" per se. Here, we measured the effects of short poly-amino-acid tags(guests) on the solubility of a host protein, a simplified bovine pancreatic trypsin inhibitor(BPTI), to which they were fused at the C-terminus. We analyzed 10 amino acid types, representing the full range of biophysical properties(acidic, basic, polar, and hydrophobic). As anticipated, positively charged residues significantly increased the solubility of the model protein, at both pH 4. 7 and 8. 7, whereas very hydrophobic poly-Ile markedly reduced the solubility of BPTI. Furthermore, to ensure that the measured solubility values were context independent and could provide a genuine "solubility propensity scale", we confirmed that the tags remained independent of the structure, thermal stability, and biochemical activity of the host protein. These observations suggest that this approach is valuable for measuring the solubility propensities of amino acids, which could eventually allow the calculation of a polypeptide's relative solubility from its amino acid sequence.
|
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
[Remarks] The first prize for the poster(Bestposter賞)受賞Mohammad Monirul Islam, KeiichiNoguchi, Masafumi Yohda, KurodaYutaka," Effect of short peptide tagson protein solubility, function, andstructure" Symposium on the Role ofBiochemists in Health and Environment, Dhaka, Bangladesh, May 21, 2010
-
[Remarks] X線結晶構造解析はPhoton factory(高エネルギー加速研究機構、KEK)で実施した(2011G108)
-
-
-
