Drug Information

General Information of This Drug
Drug ID DRG00405
Drug Name 10-Hydroxycamptothecin
Synonyms
10-Hydroxycamptothecin; 19685-09-7; (S)-10-Hydroxycamptothecin; Hydroxycamptothecin; 10-hydroxycamptothecine; 10-Hydroxy camptothecin; (S)-4-Ethyl-4,9-dihydroxy-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione; Hydroxycamptothecine; (4S)-4-Ethyl-4,9-dihydroxy-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione; Camptothecin, hydroxy-; Camptothecine, 10-hydroxy-; 10-HCPT; 10-Hydroxy-Camptothecin; NSC107124; NSC-107124; CHEMBL273862; CHEBI:81395; 9Z01632KRV; Hydroxy camptothecine; MFCD02093100; (S)-4-ethyl-4,9-dihydroxy-1,12-dihydro-14H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4H)-dione; Camptothecin, 10-hydroxy-; (20S)-4-Ethyl-4,9-dihydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione; (S)-4-Ethyl-4,9-dihydroxy-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione ((S)-10-Hydroxycamptothecin); NSC 107124; (S)-10-Hydroxycamptothecin hydrate; UNII-9Z01632KRV; CAMPTOTHECIN, 10-HYDROXY; 10-Hydroxy-CPT; Spectrum_001639; (+)-(S)-10-HYDROXYCAMPTOTHECIN; SpecPlus_000763; Spectrum2_001660; Spectrum3_001621; Spectrum4_001815; Spectrum5_000549; ethyl(dihydroxy)[?]dione; SCHEMBL25875; BSPBio_003281; KBioGR_002454; KBioSS_002119; 1H-Pyrano(3',4':6,7)indolizino(1,2-b)quinoline-3,14(4H,12H)-dione, 4-ethyl-4,9-dihydroxy-, hydrate, (S)-; DivK1c_006859; SPECTRUM1504123; SPBio_001819; KBio1_001803; KBio2_002119; KBio2_004687; KBio2_007255; KBio3_002501; DTXSID00941444; EX-A988; BCP01385; HY-N0095; (+)-10-HYDROXYCAMPTOTHECIN; BDBM50008922; CCG-38770; s2423; s3898; AKOS015919293; AC-5502; BCP9000058; CS-5193; DB12385; 10-HYDROXYCAMPTOTHECIN [WHO-DD]; NCGC00095986-01; NCGC00095986-02; NCGC00095986-03; NCGC00095986-04; NCGC00178165-01; 1H-Pyrano(3',4':6,7)indolizino(1,2-b)quinoline-3,14(4H,12H)-dione-,4-ethyl-4,9-dihydroxy-, (S)-; AC-13221; AS-13196; NCI60_000173; SY010687; H1463; NS00018317; A25382; C17939; EN300-19810684; SR-05000002620; Q-100241; SR-05000002620-1; BRD-K63784565-001-02-1; BRD-K63784565-001-03-9; BRD-K63784565-001-05-4; BRD-K63784565-001-06-2; Q27155328; Z3093896188; 4-Ethyl-4,9-dihydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione; (19S)-19-ethyl-7,19-dihydroxy-17-oxa-3,13-diazapentacyclo[11.8.0.0^{2,11}.0^{4,9}.0^{15,20}]henicosa-1(21),2(11),3,5,7,9,15(20)-heptaene-14,18-dione; (19S)-19-ethyl-7,19-dihydroxy-17-oxa-3,13-diazapentacyclo[11.8.0.02,11.04,9.015,20]henicosa-1(21),2(11),3,5,7,9,15(20)-heptaene-14,18-dione; (S)-10-Hydroxycamptothecin;-;(+/-)-4-ethyl-4,9-dihydroxy-1h-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4h,12h)-dione; (S)-4-Ethyl-4,9-dihydroxy-1H-pyrano[3 inverted exclamation mark ,4 inverted exclamation mark :6,7]indolizino[1,2-b]quinoline-3,14-(4H,12H)-dione; (S)-4-Ethyl-4,9-dihydroxy-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14-(4H,12H)-dione; 1H-PYRANO(3',4':6,7)INDOLIZINO(1,2-B)QUINOLINE-3,14(4H,12H)-DIONE, 4-ETHYL-4,9-DIHYDROXY-, (4S)-; 1H-Pyrano[3',7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione-,4-ethyl-4,9-dihydroxy-, (S)-; 4-Ethyl-4,10-dihydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione; 4-Ethyl-4,9-dihydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione (10-hydroxycamptothecin)
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Target(s) DNA topoisomerase 1 (TOP1)  Target Info 
Structure
Formula
C20H16N2O5
#Ro5 Violations (Lipinski): 0 Molecular Weight (mw) 364.4
Lipid-water partition coefficient (xlogp) 0.6
Hydrogen Bond Donor Count (hbonddonor) 2
Hydrogen Bond Acceptor Count (hbondacc) 6
Rotatable Bond Count (rotbonds) 1
PubChem CID
97226
Canonical smiles
CCC1(C2=C(COC1=O)C(=O)N3CC4=C(C3=C2)N=C5C=CC(=CC5=C4)O)O
InChI
InChI=1S/C20H16N2O5/c1-2-20(26)14-7-16-17-11(5-10-6-12(23)3-4-15(10)21-17)8-22(16)18(24)13(14)9-27-19(20)25/h3-7,23,26H,2,8-9H2,1H3/t20-/m0/s1
InChIKey
HAWSQZCWOQZXHI-FQEVSTJZSA-N
IUPAC Name
(19S)-19-ethyl-7,19-dihydroxy-17-oxa-3,13-diazapentacyclo[11.8.0.02,11.04,9.015,20]henicosa-1(21),2(11),3,5,7,9,15(20)-heptaene-14,18-dione
The activity data of This Drug
Standard Type Value Disease Model Cell line Cell line ID Ref.
Half Maximal Inhibitory Concentration (IC50) 18 nM Lymphoblastic leukemia L1210 cell CVCL_0382 [1]
Half Maximal Inhibitory Concentration (IC50) 110 nM Lung adenocarcinoma A-549 cell CVCL_0023 [2]
Half Maximal Inhibitory Concentration (IC50) 140 nM Hepatocellular carcinoma SMMC-7721 cell CVCL_0534 [3]
Half Maximal Inhibitory Concentration (IC50) 148 nM Colon carcinoma HCT 116 cell CVCL_0291 [4]
Half Maximal Inhibitory Concentration (IC50) 250 nM Acute myeloid leukemia HL-60 cell CVCL_0002 [5]
Half Maximal Inhibitory Concentration (IC50) 300 nM Lung adenocarcinoma A-549 cell CVCL_0023 [5]
Half Maximal Inhibitory Concentration (IC50) 600 nM Human papillomavirus-related endocervical adenocarcinoma KB cell CVCL_0372 [6]
Half Maximal Inhibitory Concentration (IC50) 700 nM Ovarian endometrioid adenocarcinoma A2780 cell CVCL_0134 [6]
Half Maximal Inhibitory Concentration (IC50) 800 nM Lung adenocarcinoma A-549 cell CVCL_0023 [7]
Half Maximal Inhibitory Concentration (IC50) 1.75 uM Lung adenocarcinoma A-549 cell CVCL_0023 [8]
Half Maximal Inhibitory Concentration (IC50) 2.4 uM Invasive breast carcinoma MCF-7 cell CVCL_0031 [7]
Half Maximal Inhibitory Concentration (IC50) 2.47 uM Hepatoma Bel-7402 cell CVCL_5492 [4]
Half Maximal Inhibitory Concentration (IC50) 3.2 uM Colon carcinoma HCT 116 cell CVCL_0291 [9]
Half Maximal Inhibitory Concentration (IC50) 3.5 uM Colon carcinoma HCT 116 cell CVCL_0291 [7]
Half Maximal Inhibitory Concentration (IC50) 6.55 uM Gastric cancer MGC-803 cell CVCL_5334 [10]
Half Maximal Inhibitory Concentration (IC50) 10.1 uM Hepatoblastoma Hep-G2 cell CVCL_0027 [7]
Half Maximal Inhibitory Concentration (IC50) 10.21 uM Hepatoblastoma Hep-G2 cell CVCL_0027 [11]
Half Maximal Inhibitory Concentration (IC50) 11.83 uM Bladder carcinoma T24 cell CVCL_0554 [8]
Half Maximal Inhibitory Concentration (IC50) 20.4 uM Cervical carcinoma L02 cell CVCL_6926 [9]
Half Maximal Inhibitory Concentration (IC50) 48.2 uM Invasive breast carcinoma MCF-7 cell CVCL_0031 [12]
Each Peptide-drug Conjugate Related to This Drug
Full Information of The Activity Data of The PDC(s) Related to This Drug
R-L-HCPT [Investigative]
 PDC Info 
Discovered Using Cell Line-derived Xenograft Model
Click To Hide/Show 2 Activity Data Related to This Level
Experiment 1 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Tumer volume 700 mm3
Administration Time 10 days
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

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Description
Compared with the tumors in the control group with a final tumor volume of 3800 mm3, the tumors in the R-L-HCPT group grew much more slowly, and the mean tumor volume expanded from 200 to 700 mm3 within 10 days.
In Vivo Model Murine melanoma B16-F10 xenograft model in BALB/c mice.
Experiment 2 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Body weight 31g
Administration Time 10 days
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

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Description
Notably, there were no significant body weight losses (Figure 6D), suggesting that R-L-HCPT did not induce systemic toxicity.
In Vivo Model Murine melanoma B16-F10 xenograft model in BALB/c mice.
Revealed Based on the Cell Line Data
Click To Hide/Show 13 Activity Data Related to This Level
Experiment 1 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 1.1 μM
Administration Time 48 h
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

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Description
The cytotoxic activity of R-L-HCPT on MHCC-97H cells was time-dependent. With R-L-HCPT treatment for 6 and 12 h, the IC50 values were 13.5 μM and 11.7 μM, respectively. However, when the incubation time was extended to 24 and 48 h, the IC50 values were greatly reduced to 3.12 μM and 1.1 μM, respectively.
In Vitro Model Hepatocellular carcinoma MHCC97H cell CVCL_4972
Experiment 2 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 2.8 ± 0.4 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

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Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Amelanotic melanoma LO #2 cell CVCL_C7SD
Experiment 3 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 2.9 ± 0.5 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Hepatoblastoma Hep-G2 cell CVCL_0027
Experiment 4 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 3.12 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

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Description
The IC50 values for R-lycosin-I, R-L-HCPT conjugates, and HCPT were 15.27, 3.12, and 23.83 μM, respectively.
In Vitro Model Hepatocellular carcinoma MHCC97H cell CVCL_4972
Experiment 5 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 3.12 μM
Administration Time 24 h
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
The cytotoxic activity of R-L-HCPT on MHCC-97H cells was time-dependent. With R-L-HCPT treatment for 6 and 12 h, the IC50 values were 13.5 μM and 11.7 μM, respectively. However, when the incubation time was extended to 24 and 48 h, the IC50 values were greatly reduced to 3.12 μM and 1.1 μM, respectively.
In Vitro Model Hepatocellular carcinoma MHCC97H cell CVCL_4972
Experiment 6 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 3.9 ± 0.4 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Lung adenocarcinoma A-549 cell CVCL_0023
Experiment 7 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 4.4 ± 0.5 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Normal BEAS-2B cell CVCL_0168
Experiment 8 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 4.9 ± 0.3 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Breast adenocarcinoma MDA-MB-231 cell CVCL_0062
Experiment 9 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 5.8 ± 1.1 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Normal HEK-293T cell CVCL_0063
Experiment 10 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 6.1 ± 0.1 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Mouse melanoma B16-F10 cell CVCL_0159
Experiment 11 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 6.6 ± 0.3 μM
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
In addition, as shown in Table 1, the other cancer cell lines (HeLa, MDA-MB-231, B16-F10, HepG2, and A549) and noncancer cell lines (HEK293t, Beas-2B, and LO2) were evaluated in the cytotoxicity test. The IC50 values of R-L-HCPT were 2.9-6.6 μM for cancer cell lines and 2.8-5.8 μM for noncancer cell lines.
In Vitro Model Human papillomavirus-related cervical adenocarcinoma HeLa cell CVCL_0030
Experiment 12 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 11.7 μM
Administration Time 12 h
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

   Click to Show/Hide
Description
The cytotoxic activity of R-L-HCPT on MHCC-97H cells was time-dependent. With R-L-HCPT treatment for 6 and 12 h, the IC50 values were 13.5 μM and 11.7 μM, respectively. However, when the incubation time was extended to 24 and 48 h, the IC50 values were greatly reduced to 3.12 μM and 1.1 μM, respectively.
In Vitro Model Hepatocellular carcinoma MHCC97H cell CVCL_4972
Experiment 13 Reporting the Activity Data of This PDC [13]
Indication Solid tumor
Efficacy Data Half maximal inhibitory concentration (IC50) 13.5 μM
Administration Time 6 h
MOA of PDC
Our previous studies demonstrated that R-lycosin-I was a typical cationic anticancer peptide that contained a high relative abundance of positively charged arginine residues and possessed an amphiphilic character to allow its assembly into nanostructures in aqueous environments. Herein, we designed and synthesized a self-assembling anticancer conjugate in which R-lycosin-I covalently coupled with HCPT, a DNA topoisomerase I inhibitor through the glutamic anhydride linker. This conjugate (R-L-HCPT) could spontaneously associate into uniform 40-60 nm nanospheres in aqueous solution. The R-L-HCPT nanospheres exhibited excellent antitumor growth activity and antimetastatic efficacy compared with free HCPT or free R-lycosin-I in vitro and in vivo. Our study might provide new opportunities for the development of a self-assembling peptide-drug delivery system that could synergistically enhance anticancer outcomes.

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Description
The cytotoxic activity of R-L-HCPT on MHCC-97H cells was time-dependent. With R-L-HCPT treatment for 6 and 12 h, the IC50 values were 13.5 μM and 11.7 μM, respectively. However, when the incubation time was extended to 24 and 48 h, the IC50 values were greatly reduced to 3.12 μM and 1.1 μM, respectively.
In Vitro Model Hepatocellular carcinoma MHCC97H cell CVCL_4972
References
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