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BBI(Bowman-Birk type proteinase inhibitor)
General Information
DCTPep ID DCTPep00228
Peptide Name BBI(Bowman-Birk type proteinase inhibitor)
Sequence DDESSKPCCDQCACTKSNPPQCRCSDMRLNSCHSACKSCICALSYPAQCFCVDITDFCYEPCKPSEDDKEN
Sequence Length 71
UniProt ID Not available
PubChem CID Not available
Origin Glycine max
Type Native peptide
Classification
ACP Tumor active peptide
Activity Information
| Cell Line | Disease | Activity | Assay | Testing Time | Literature |
|---|---|---|---|---|---|
| HT-29 | Colon adenocarcinoma | IC50=48.3±3.5µM | NR uptake assay | 24-96h | 1 |
Hemolytic Activity Not available
Normal (non-cancerous) Cytotoxicity Not available
Target Not available
Affinity Not available
Mechanism Not available
Structure Information
PDB ID Not available
Predicted Structure DCTPep00228
(Please note that there is the predicted structure, predicted by AlphaFold)
Helicity Not available
Linear/Cyclic Cyclic
Disulfide/Other Bond Cys8<--->Cys62; Cys9<--->Cys24; Cys12<--->Cys58; Cys14<--->Cys22; Cys32<--->Cys39; Cys36<--->Cys51; Cys41<--->Cys49
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Chiral L
Physicochemical Information
Formula C316H492N90O115S15
Absent amino acids GW
Theoretical pI 4.51
Acidic residues 12
Basic residues 8
Polar residues 30
Molecular weight (Average) 7872.82
Molecular weight (Monoisotopic) 7867.12
Common amino acids C
Net charge -4
Instability index (II) 54.07
Aliphatic index 31.69
Grand average of hydropathicity (GRAVY) -0.634
Half Life
1.1 hours (mammalian reticulocytes, in vitro).
3 min (yeast, in vivo).
>10 hours (Escherichia coli, in vivo).
Extinction coefficients
Ext. coefficient 3855
Abs 0.1% (=1 g/l) 0.490, assuming all pairs of Cys residues form cystines
Ext. coefficient 2980
Abs 0.1% (=1 g/l) 0.379, assuming all Cys residues are reduced
Amino acid distribution
Literature Information
Literature 1
Pubmed ID 19885848
Title The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases
Year 2010
Patent
Patent ID Not available
Patent Title Not available
Other Iinformation Not available
Other Published ID Not available
This work is licensed under a Creative Commons Attribution 4.0 International License.