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GRRRRSVQWCA details |
| Primary information | |
|---|---|
| ID | antitb_1164, |
| Name | 24709266 |
| N-Terminal modification | hLFcin1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Protein Derived |
| Strain | From human lactoferrin |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium strain 2447 smooth transparent variant (SmT) |
| Cell Line | IC50 = 15.8 ± 4.5 |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | None |
| In vivo Model | NA |
| Lethal Dose | NA |
| Immune Responce | None |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | Permeabilization of peptide causes significant changes both in the surface and in the ultrastructural organization of the mycobacterial cells. |
| Other activities | Cell envelope |
| PMID | None |
| Year of Publication | Antibacterial |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1165, |
| Name | 24709266 |
| N-Terminal modification | hLFcin1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Protein Derived |
| Strain | From human lactoferrin |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium strain 2447 smooth transparent variant (SmT) |
| Cell Line | IC90 =34.6 ± 22.4 |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | None |
| In vivo Model | NA |
| Lethal Dose | NA |
| Immune Responce | None |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | Permeabilization of peptide causes significant changes both in the surface and in the ultrastructural organization of the mycobacterial cells. |
| Other activities | Cell envelope |
| PMID | None |
| Year of Publication | Antibacterial |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1166, |
| Name | 24709266 |
| N-Terminal modification | hLFcin1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Protein Derived |
| Strain | From human lactoferrin |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium strain 2-151 smooth transparent variant (SmT) |
| Cell Line | IC50 = 11.0 ± 4.1 |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | None |
| In vivo Model | NA |
| Lethal Dose | NA |
| Immune Responce | None |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | Permeabilization of peptide causes significant changes both in the surface and in the ultrastructural organization of the mycobacterial cells. |
| Other activities | Cell envelope |
| PMID | None |
| Year of Publication | Antibacterial |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1167, |
| Name | 24709266 |
| N-Terminal modification | hLFcin1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Protein Derived |
| Strain | From human lactoferrin |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium strain 2-151 smooth transparent variant (SmT) |
| Cell Line | IC90 = 65.8 ± 19.3 |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | None |
| In vivo Model | NA |
| Lethal Dose | NA |
| Immune Responce | None |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | Permeabilization of peptide causes significant changes both in the surface and in the ultrastructural organization of the mycobacterial cells. |
| Other activities | Cell envelope |
| PMID | None |
| Year of Publication | Antibacterial |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1168, |
| Name | 24709266 |
| N-Terminal modification | hLFcin1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Protein Derived |
| Strain | From human lactoferrin |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium strain 2-151 smooth doomed variant (SmD) |
| Cell Line | IC50 = 15.2 ± 2.9 |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | None |
| In vivo Model | NA |
| Lethal Dose | NA |
| Immune Responce | None |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | Permeabilization of peptide causes significant changes both in the surface and in the ultrastructural organization of the mycobacterial cells. |
| Other activities | Cell envelope |
| PMID | None |
| Year of Publication | Antibacterial |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1169, |
| Name | 24709266 |
| N-Terminal modification | hLFcin1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Protein Derived |
| Strain | From human lactoferrin |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium strain 2-151 smooth doomed variant (SmD) |
| Cell Line | IC90 =37.9 ± 15.9 |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | None |
| In vivo Model | NA |
| Lethal Dose | NA |
| Immune Responce | None |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | Permeabilization of peptide causes significant changes both in the surface and in the ultrastructural organization of the mycobacterial cells. |
| Other activities | Cell envelope |
| PMID | None |
| Year of Publication | Antibacterial |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1893, |
| Name | 24709266 |
| N-Terminal modification | Human lactoferricin 1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Natural |
| Strain | Derived from human lactoferricin protein |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium 2447 smT |
| Cell Line | IC50 = 15.8 ± 4.5 μM |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | NA |
| In vivo Model | Tratment with this concentration inhibit 50% bacterial growth |
| Lethal Dose | NA |
| Immune Responce | NA |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | NA |
| Other activities | Lipid bilayer |
| PMID | NA |
| Year of Publication | NA |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1894, |
| Name | 24709266 |
| N-Terminal modification | Human lactoferricin 1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Natural |
| Strain | Derived from human lactoferricin protein |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium 2447 smT |
| Cell Line | IC90 = 34.6 ± 22.4 μM |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | NA |
| In vivo Model | Tratment with this concentration inhibit 90% bacterial growth |
| Lethal Dose | NA |
| Immune Responce | NA |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | NA |
| Other activities | Lipid bilayer |
| PMID | NA |
| Year of Publication | NA |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1895, |
| Name | 24709266 |
| N-Terminal modification | Human lactoferricin 1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Natural |
| Strain | Derived from human lactoferricin protein |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium 2-151 smT |
| Cell Line | IC50 = 11.0 ± 4.1 μM |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | NA |
| In vivo Model | Tratment with this concentration inhibit 50% bacterial growth |
| Lethal Dose | NA |
| Immune Responce | NA |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | NA |
| Other activities | Lipid bilayer |
| PMID | NA |
| Year of Publication | NA |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1896, |
| Name | 24709266 |
| N-Terminal modification | Human lactoferricin 1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Natural |
| Strain | Derived from human lactoferricin protein |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium 2-151 smT |
| Cell Line | IC90 = 65.8 ± 19.13 μM |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | NA |
| In vivo Model | Tratment with this concentration inhibit 90% bacterial growth |
| Lethal Dose | NA |
| Immune Responce | NA |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | NA |
| Other activities | Lipid bilayer |
| PMID | NA |
| Year of Publication | NA |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1897, |
| Name | 24709266 |
| N-Terminal modification | Human lactoferricin 1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Natural |
| Strain | Derived from human lactoferricin protein |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium 2-151 smD |
| Cell Line | IC50 = 15.2± 2.9 μM |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | NA |
| In vivo Model | Tratment with this concentration inhibit 50% bacterial growth |
| Lethal Dose | NA |
| Immune Responce | NA |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | NA |
| Other activities | Lipid bilayer |
| PMID | NA |
| Year of Publication | NA |
| Tertiary Structure (Technique) | Not Predicted), |
| Primary information | |
|---|---|
| ID | antitb_1898, |
| Name | 24709266 |
| N-Terminal modification | Human lactoferricin 1-11 |
| C-Terminal Modification | GRRRRSVQWCA |
| Chemical Modification | Free |
| Linear/Cyclic | Free |
| Length | None |
| Chirality | Linear |
| Nature | 11 |
| Source | L |
| Origin | Cationic |
| Species | Natural |
| Strain | Derived from human lactoferricin protein |
| Inhibition Concentration | Mycobacterium avium |
| In Vitro/ In vivo | Mycobacterium avium 2-151 smD |
| Cell Line | IC90 = 37.9 ± 15.9 μM |
| Inhibition Concentration | In vitro |
| Sequence | 2014 |
| Cytotoxicity | NA |
| In vivo Model | Tratment with this concentration inhibit 90% bacterial growth |
| Lethal Dose | NA |
| Immune Responce | NA |
| Mechanism of Action | NA |
| Target | NA |
| Combination Therapy | NA |
| Other activities | Lipid bilayer |
| PMID | NA |
| Year of Publication | NA |
| Tertiary Structure (Technique) | Not Predicted), |