Peptide Information

General Information of This Peptide
Peptide ID
PEP00094
Peptide Name
ABD-RGDK
Structure
Sequence
MGCGSLAEAKVLANRELDKYGVSDFYKRLINKAKTVEGVEALKLHILAALPGGGSGGGSGGGSSRGDK
Peptide Type
Linear
PDC Transmembrane Types Cell-penetrating peptides (CPPs)
Formula
C297H492N88O94S2
Isosmiles
[H]NCCCC[C@H](NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@H](CCC/N=C(\N)N[H])NC(=O)[C@H](CO[H])NC(=O)[C@H](CO[H])NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](CO[H])NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](CO[H])NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@]([H])(NC(=O)[C@H](Cc1cn([H])cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN[H])NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@@]([H])(NC(=O)[C@H](CCCCN[H])NC(=O)[C@H](C)NC(=O)[C@H](CCCCN[H])NC(=O)[C@H](CC(=O)N[H])NC(=O)[C@@]([H])(NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC/N=C(\N)N[H])NC(=O)[C@H](CCCCN[H])NC(=O)[C@H](Cc1ccc(O[H])cc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CO[H])NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](Cc1ccc(O[H])cc1)NC(=O)[C@H](CCCCN[H])NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC/N=C(\N)N[H])NC(=O)[C@H](CC(=O)N[H])NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN[H])NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO[H])NC(=O)CNC(=O)[C@H](CS[H])NC(=O)CNC(=O)[C@H](CCSC)N[H])C(C)C)C(C)C)[C@@H](C)CC)[C@@H](C)O[H])C(C)C)C(C)C)[C@@H](C)CC)C(=O)O
InChI
InChI=1S/C297H492N88O94S2/c1-38-155(27)238(290(474)373-188(105-145(7)8)268(452)337-157(29)241(425)333-158(30)247(431)375-202(110-150(17)18)293(477)385-101-60-73-210(385)285(469)331-126-218(402)320-123-215(399)322-128-220(404)342-204(136-387)253(437)325-124-216(400)318-121-213(397)321-127-219(403)341-203(135-386)252(436)326-125-217(401)319-122-214(398)323-129-221(405)343-206(138-389)282(466)376-207(139-390)283(467)349-172(70-57-98-315-295(308)309)249(433)327-131-222(406)340-199(117-231(419)420)276(460)359-185(294(478)479)69-49-56-97-304)383-280(464)196(114-168-120-314-142-332-168)369-270(454)190(107-147(11)12)362-260(444)175(65-45-52-93-300)352-269(453)189(106-146(9)10)360-245(429)162(34)336-257(441)183(84-88-229(415)416)358-286(470)234(151(19)20)378-225(409)133-328-250(434)181(82-86-227(411)412)357-288(472)237(154(25)26)381-292(476)240(164(36)392)384-265(449)178(68-48-55-96-303)347-242(426)159(31)334-255(439)173(63-43-50-91-298)351-275(459)198(116-212(307)396)374-291(475)239(156(28)39-2)382-279(463)192(109-149(15)16)364-262(446)180(72-59-100-317-297(312)313)350-258(442)174(64-44-51-92-299)353-272(456)195(113-167-76-80-170(394)81-77-167)367-273(457)194(111-165-61-41-40-42-62-165)368-278(462)201(119-233(423)424)371-284(468)208(140-391)377-287(471)235(152(21)22)379-226(410)134-329-251(435)193(112-166-74-78-169(393)79-75-166)366-261(445)176(66-46-53-94-301)354-277(461)200(118-232(421)422)370-271(455)191(108-148(13)14)363-263(447)184(85-89-230(417)418)356-259(443)179(71-58-99-316-296(310)311)355-274(458)197(115-211(306)395)361-246(430)163(35)339-267(451)187(104-144(5)6)372-289(473)236(153(23)24)380-264(448)177(67-47-54-95-302)346-243(427)160(32)335-256(440)182(83-87-228(413)414)348-244(428)161(33)338-266(450)186(103-143(3)4)365-281(465)205(137-388)344-223(407)132-330-254(438)209(141-480)345-224(408)130-324-248(432)171(305)90-102-481-37/h40-42,61-62,74-81,120,142-164,171-210,234-240,386-394,480H,38-39,43-60,63-73,82-119,121-141,298-305H2,1-37H3,(H2,306,395)(H2,307,396)(H,314,332)(H,318,400)(H,319,401)(H,320,402)(H,321,397)(H,322,399)(H,323,398)(H,324,432)(H,325,437)(H,326,436)(H,327,433)(H,328,434)(H,329,435)(H,330,438)(H,331,469)(H,333,425)(H,334,439)(H,335,440)(H,336,441)(H,337,452)(H,338,450)(H,339,451)(H,340,406)(H,341,403)(H,342,404)(H,343,405)(H,344,407)(H,345,408)(H,346,427)(H,347,426)(H,348,428)(H,349,467)(H,350,442)(H,351,459)(H,352,453)(H,353,456)(H,354,461)(H,355,458)(H,356,443)(H,357,472)(H,358,470)(H,359,460)(H,360,429)(H,361,430)(H,362,444)(H,363,447)(H,364,446)(H,365,465)(H,366,445)(H,367,457)(H,368,462)(H,369,454)(H,370,455)(H,371,468)(H,372,473)(H,373,474)(H,374,475)(H,375,431)(H,376,466)(H,377,471)(H,378,409)(H,379,410)(H,380,448)(H,381,476)(H,382,463)(H,383,464)(H,384,449)(H,411,412)(H,413,414)(H,415,416)(H,417,418)(H,419,420)(H,421,422)(H,423,424)(H,478,479)(H4,308,309,315)(H4,310,311,316)(H4,312,313,317)/t155-,156-,157-,158-,159-,160-,161-,162-,163-,164+,171-,172-,173-,174-,175-,176-,177-,178-,179-,180-,181-,182-,183-,184-,185-,186-,187-,188-,189-,190-,191-,192-,193-,194-,195-,196-,197-,198-,199-,200-,201-,202-,203-,204-,205-,206-,207-,208-,209-,210-,234-,235-,236-,237-,238-,239-,240-/m0/s1
InChIKey
COXLXEVQIJOWNR-QPCLHCDQSA-N
Pharmaceutical Properties
Molecule Weight
6863.859
Polar area
2937.6
Complexity
6859.586544
xlogp Value
-35.7295
Heavy Count
481
Rot Bonds
257
Hbond acc
100
Hbond Donor
101
The Activity Data of This Peptide
Peptide Activity Information 1 [1]
A280nm 0 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

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Experimental Condition Transferrin(ABD-RGDK: Tf 1: 0)
Peptide Activity Information 2 [1]
A280nm 0 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

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Experimental Condition Human serum albumin(ABD-RGDK: HSA 1: 0)
Peptide Activity Information 3 [1]
A280nm 75 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Transferrin(ABD-RGDK: Tf 1: 1)
Peptide Activity Information 4 [1]
A280nm 75 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Human serum albumin(ABD-RGDK: HSA 1: 1)
Peptide Activity Information 5 [1]
A280nm 80 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Human serum albumin(ABD-RGDK: HSA 1: 2)
Peptide Activity Information 6 [1]
A280nm 170 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Transferrin(ABD-RGDK: Tf 1: 2)
Peptide Activity Information 7 [1]
A280nm 230 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Human serum albumin(ABD-RGDK: HSA 1: 5)
Peptide Activity Information 8 [1]
A280nm 440 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Transferrin(ABD-RGDK: Tf 1: 5)
Peptide Activity Information 9 [1]
A280nm 670 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

   Click to Show/Hide
Experimental Condition Human serum albumin(ABD-RGDK: HSA 1: 10)
Peptide Activity Information 10 [1]
A280nm 800 mAU
Binding Affinity Assay
To verify the binding affinity of the fusion peptides to serum albumin, we mixed the ABD-RGDK and ABD-RPARPAR fusion peptides with human serum albumin and transferrin in different molar ratios (1:0, 1:1, 1:2, 1:5, 1:10), separately. The concentration of fusion peptides in different groups should remain consistent. After mixing for 5 min, 500 μL of mixture was analyzed by a Superdex 75 HR column (10 300 mm ID, GE Healthcare) which was equilibrated and eluted with 20 mM PB, 0.1 M Na2SO4, pH 7.0. The peak heights of fusion peptides in various conditions were measured and compared to validate its binding affinity and the specificity to HSA.

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Experimental Condition Transferrin(ABD-RGDK: Tf 1: 10)
Each Peptide-drug Conjugate Related to This Peptide
Full Information of The Activity Data of The PDC(s) Related to This Peptide
ABD-RGDK-DOXO [Investigative]
 PDC Info 
Obtained from the Model Organism Data
Click To Hide/Show 1 Activity Data Related to This Level
Experiment 1 Reporting the Activity Data of This PDC [1]
Indication Tumor
Efficacy Data Retarded the tumor growth rate
47.78%
Administration Time 20 days
Administration Dosage 3.0 mg/kg doxorubicin equivalent
Description
The doxorubicin, DOXO-EMCH, ABD-RGDK-DOXO, and ABD-RPARPAR-DOXO retarded the tumor growth rate by 24.28, 25.67, 47.78, and 47.09% on day 20, respectively.
In Vivo Model Tumor-bearing BALB/c nude mice.
Half life period 23.67 ± 0.35 h
Revealed Based on the Cell Line Data
Click To Hide/Show 1 Activity Data Related to This Level
Experiment 1 Reporting the Activity Data of This PDC [1]
Indication Tumor
Efficacy Data Half Maximal Inhibitory Concentration (IC50)
9.27 ± 3.56 µM
Evaluation Method CCK-8 assay
Description
Whereas conjugation of a peptide would hinder the passive diffusion route, resulting in higher IC50 values for the peptide-DOX-conjugates (9.27 ± 3.56 uM for ABD-RGDK-DOXO and 11.21 ± 4.54 uM for ABD-RPARPAR-DOXO, respectively).
In Vitro Model Lung adenocarcinoma A-549 cell CVCL_0023
Half life period 23.67 ± 0.35 h
References
Ref 1 Albumin Binding Domain Fusing R/K-X-X-R/K Sequence for Enhancing Tumor Delivery of Doxorubicin. Mol Pharm. 2017 Nov 6;14(11):3739-3749. doi: 10.1021/acs.molpharmaceut.7b00497. Epub 2017 Oct 9.