Abstract
Inga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds. ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM). Circular dichroism analysis revealed that this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors. ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by Tm of 70.0 ºC and ΔG25 of 48.5 ± 0.7 kJ.mol-1. The values of ΔG25 at pH 1.6 (22.5 ± 1.2 kJ.mol-1) and pH 10.0 (31.5 ± 1.0 kJ.mol-1) indicate a reduced structural stability of the protein under these conditions. This is likely to result from pKa differences of the acid and basic side chains reflecting the changes in the non-covalent interactions in the folded state.
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Claims 7
Claim · model-written summary
ICTI was purified as a single polypeptide chain from Inga cylindrica seeds.
- Taxon
- Inga cylindrica
Inga cylindricae0 - Organ / stage
- seedse0
- Gene
- Inga cylindrica Trypsin Inhibitor (ICTI)e0
- Outcome
- single polypeptide chaine0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Inga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds.”
Claim · model-written summary
ICTI has a mass of 19.5 kDa.
- Taxon
- Inga cylindricaInga cylindricae1
- Gene
- ICTIe0
- Outcome
- proteine0
- Value
- 19.5 kDae0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM).”
e1“Inga cylindrica Trypsin Inhibitor (ICTI)”
Claim · model-written summary
ICTI inhibits bovine trypsin with Ki of 4.3 nM.
- Taxon
- Inga cylindricaInga cylindricae1
- Gene
- ICTIe0
- Outcome
- inhibitory activity against bovine trypsine0
- Value
- 4.3 nMe0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM).”
e1“Inga cylindrica Trypsin Inhibitor (ICTI)”
Claim · model-written summary
ICTI is a beta type protein with reported strand, turn and helix proportions.
- Taxon
- Inga cylindricaInga cylindricae1
- Gene
- ICTIe1
- Outcome
- β type proteine0
- Qualifier
- 40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helixe0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors.”
e1“Inga cylindrica Trypsin Inhibitor (ICTI)”
Claim · model-written summary
ICTI had its highest thermal stability at pH 7.0 within pH 1.6 to 10.0.
- Taxon
- Inga cylindricaInga cylindricae1
- Gene
- ICTIe0
- Outcome
- highest stabilitye0
- Value
- 70.0 ºCe0
- Qualifier
- pH 7.0e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by Tm of 70.0 ºC and ΔG25 of 48.5 ± 0.7 kJ.mol-1.”
e1“Inga cylindrica Trypsin Inhibitor (ICTI)”
Claim · model-written summary
ICTI had reduced structural stability at pH 1.6 and 10.0.
- Taxon
- Inga cylindricaInga cylindricae1
- Gene
- ICTIe1
- Outcome
- structural stabilitye0
- Direction
- reducede0
- Qualifier
- pH 1.6e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The values of ΔG25 at pH 1.6 (22.5 ± 1.2 kJ.mol-1) and pH 10.0 (31.5 ± 1.0 kJ.mol-1) indicate a reduced structural stability of the protein under these conditions.”
e1“Inga cylindrica Trypsin Inhibitor (ICTI)”
Claim · model-written summary
The authors attribute pH dependent stability to side chain pKa and folded-state noncovalent interactions.
- Taxon
- Inga cylindricaInga cylindricae1
- Outcome
- changes in the non-covalent interactions in the folded statee0
- Qualifier
- pKa differences of the acid and basic side chainse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“This is likely to result from pKa differences of the acid and basic side chains reflecting the changes in the non-covalent interactions in the folded state.”
e1“Inga cylindrica Trypsin Inhibitor (ICTI)”