Table 2.
Physico-chemical properties of the bLFcin, hLFcin, cLFcin, and ConLFcin peptides.
Property | bLFcin | hLFcin | cLFcin | ConLFcin |
---|---|---|---|---|
Number of amino acids | 30 | 30 | 30 | 30 |
36* | 36* | 36* | 36* | |
Molecular weight (Daltons) | 3655.47 | 3576.28 | 3542.26 | 3737.58 |
4478.31* | 4399.12* | 4365.11* | 4560.42* | |
Theoretical pI | 10.90 | 10.33 | 10.57 | 11.63 |
Total number of positively charged residues (Aspartic acid (D) + Glutamic acid (E)) | 8 | 7 | 9 | 11 |
Total number of negatively charged residues (Arginine (R) + Lysine (K)) | 1 | 1 | 1 | 1 |
Total number of atoms | 520 | 504 | 503 | 535 |
622* | 606* | 605* | 637* | |
Aliphatic index | 71.67 | 58.33 | 45.33 | 48.67 |
59.72* | 48.61* | 37.78* | 40.56* | |
Grand average of hydropathicity (GRAVY) | −0.177 | −0.717 | −0.787 | −0.863 |
−0.681* | −1.131* | −1.189* | −1.253* | |
+Estimated half-life | −1.1 h (mammalian reticulocytes, in vitro). | −7.2 h (mammalian reticulocytes, in vitro). | −1.9 h (mammalian reticulocytes, in vitro). | −1.9 h (mammalian reticulocytes, in vitro). |
−3 min (yeast, in vivo). | - >20 h (yeast, in vivo). | - >20 h (yeast, in vivo). | - >20 h (yeast, in vivo). | |
−2 min (Escherichia coli, in vivo). | - >10 h (Escherichia coli, in vivo) | - >10 h (Escherichia coli, in vivo). | - >10 h (Escherichia coli, in vivo). | |
∼Instability index | 81.25 | 55.90 | 44.28 | 80.60 |
72.80* | 51.68* | 42.00* | 72.26* | |
Atomic Formula | C164H265N51O36S4 | C154H256N50O40S4 | C151H258N50O40S4 | C163H275N57O36S4 |
C200H307N69O42S4* | C190H298N68O46S4* | C187H300N68O46S4* | C199H317N75O42S4* |
+Estimated half-life: N-terminal of the hLFcin, bLFcin, cLFcin, and ConLFcin sequences are C (Cysteine).
∼Instability index of the hLFcin, bLFcin, cLFcin, and ConLFcin peptides is computed to be 55.90, 81.25, 44.28, and 80.60, respectively. This classifies the peptides as unstable.
Calculated values for peptides tagged with 6xHis-tag. The remaining data did not change after tagging of peptides.