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Purity: ≥98%
Aprotinin is a novel and potent small protein serine protease / bovine pancreatic trypsin inhibitor (BPTI) with antifibrinolytic activity. It has a Kis of 0.06 pM and 9 nM for trypsin and chymotrypsin inhibition, respectively. The use of aprotinin lowers transfusion and perioperative blood loss. Aprotinin use was associated with a higher percentage of patients with doubled serum creatinine levels, but did not significantly increase the risk of renal failure or the need for postoperative renal replacement. Renal failure was not mentioned in the death adjudication as a factor in the death linked to aprotinin use. According to Brown and colleagues' meta-analysis, high-dose aprotinin did not significantly increase the risk of renal failure.
| Targets |
Thrombin; Trypsin (Kd = 0.06 pM); kallikrein (Kd = 0.8 nM); chymotrypsin (Kd = 9.5 nM); trypsinogen (Kd = 2 μM)
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| ln Vitro |
Aprotinin is a molecule that prevents the action of trypsin and other related proteolytic enzymes. Aprotinin is used as an enzyme inhibitor in cell biology to stop protein degradation that occurs during cell lysis or homogenization. The concentration-dependent inhibition of fibrinolytic activity and the prolonged coagulation time occur when aprotinin is present. In vitro, aprotinin effectively inhibits the contact (intrinsic) coagulation pathway[2].
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| ln Vivo |
Aprotinin prolongs the coagulation time in human plasma and inhibits clot lysis in vitro and in vivo rat tail bleeding time. Aprotinin lowers thrombus weight in a rat model of arteriovenous shunt [2].
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| Enzyme Assay |
Fibrinolysis was inhibited by aprotinin (IC(50), 0.16 +/- 0.02 micromol L(-1)) and tranexamic acid (IC(50), 24.1 +/-1.1 micromol L(-1)). In vivo, aprotinin dose-dependently reduced rat-tail bleeding time (minimal effective dose, 3 mg kg(-1) bolus plus 6 mg kg(-1 )h(-1) infusion); tranexamic acid reduced bleeding time (minimal effective dose, 100 mg kg(-1) h(-1)). In vitro, coagulation time was doubled by aprotinin at 3.2 +/- 0.2 micromol L(-1), while tranexamic acid showed no effect at concentrations up to 3 mmol L(-1). Aprotinin inhibited thrombus formation in vivo in a dose-dependent manner (minimal effective dose, 3 mg kg(-1) bolus plus 6 mg kg(-1) h(-1) infusion). Conversely, tranexamic acid dose-dependently increased thrombus formation and thrombus weight (minimal effective dose, 100 mg kg(-1 )h(-1) infusion) [2].
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| Cell Assay |
Mouse G8-1 myoblasts are cultured in maintenance medium (DMEM + 20% FBS) without differentiation. Different protease inhibitors are added to the culture media when the cells reach about 40–50% confluence, and the cells are then incubated for an additional night. After that, the cells are placed in a 7-day incubation period using differentiation-promoting medium (DMEM + 10% horse serum ± protease inhibitor).
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| Animal Protocol |
Rats: In the study, male Wistar rats weighing 180–220 g are employed. Physiological saline dissolves aprotinin. A maintenance infusion is given after a bolus injection of aprotinin. 1.5 mg kg-1 and 3 mg kg-1 h-1, 3 mg kg-1 and 6 mg kg-1 h-1, up to 5 mg kg-1 and 10 mg kg-1 h-1, are the doses that are administered. Pharmacokinetic studies in rats are used to determine the plasma concentrations of the two agents[4].
Mice: The study employed an intact mouse model of ischemia/reperfusion (30 min-I/60 min-R), and the mice were divided into four groups: wild type (WT, C57BL/6; n = 10), WT mice with aprotinin (4mL/kg; n = 10), transgenic mice lacking the TNFRI (TNFRInull; n = 10), and TNFRInull with aprotinin (n = 10)[6].
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| ADME/Pharmacokinetics |
Absorption, Distribution and Excretion
100% (IV) Following a single IV dose of radiolabelled aprotinin, approximately 25-40% of the radioactivity is excreted in the urine over 48 hours. After a 30 minute infusion of 1 million KIU, about 2% is excreted as unchanged drug. After a larger dose of 2 million KIU infused over 30 minutes, urinary excretion of unchanged aprotinin accounts for approximately 9% of the dose. After intravenous (iv) injection, rapid distribution of aprotinin occurs into the total extracellular space, leading to a rapid initial decrease in plasma aprotinin concentration. Following a single iv dose of radiolabelled aprotinin, approximately 25-40% of the radioactivity is excreted in the urine over 48 hours. After a 30 minute infusion of 1 million KIU, about 2% is excreted as unchanged drug. After a larger dose of 2 million KIU infused over 30 minutes, urinary excretion of unchanged aprotinin accounts for approximately 9% of the dose. Animal studies have shown that aprotinin is accumulated primarily in the kidney. Aprotinin, after being filtered by the glomeruli, is actively reabsorbed by the proximal tubules in which it is stored in phagolysosomes. There are no available studies on the distribution of aprotinin into breast milk. For more Absorption, Distribution and Excretion (Complete) data for APROTININ (9 total), please visit the HSDB record page. Metabolism / Metabolites Aprotinin is slowly degraded by lysosomal enzymes. Aprotinin is slowly degraded by lysosomal enzymes. The physiological renal handling of aprotinin is similar to that of other small proteins, e.g., insulin. Biological Half-Life Following this distribution phase, a plasma half-life of about 150 minutes is observed. At later time points, (i.e., beyond 5 hours after dosing) there is a terminal elimination phase with a half-life of about 10 hours. Following this distribution phase, a plasma half-life of about 150 minutes is observed. At later time points, (i.e., beyond 5 hours after dosing) there is a terminal elimination phase with a half-life of about 10 hours. |
| References | |
| Additional Infomation |
Aprotinin is a protein-based drug that is also known as bovine pancreatic trypsin inhibitor (BPTI). Since it demonstrates the capacity to slow fibrinolysis, it has been employed to reduce bleeding during complex surgery such as heart and liver surgery. For this use, it is typically administered by injection. The goal of using of aprotinin was subsequently to minimize end-organ damage resulting from hypotension due to blood loss in surgery and to reduce the necessity for blood transfusions during surgery. Nevertheless, the drug was formally withdrawn worldwide in May of 2008 after studies confirmed that its use enhanced the risk of complications or death. The substance is consequently made available only for very restricted research use.
Aprotinin is a single chain polypeptide isolated from bovine lung with antifibrinolytic and anti-inflammatory activities. As a broad-spectrum serine protease inhibitor, aprotinin bovine competitively and reversibly inhibits the activity of a number of different esterases and proteases, including trypsin, chymotrypsin, kallikrein, plasmin, tissue plasminogen activator, and tissue and leukocytic proteinases, resulting in attenuation of the systemic inflammatory response (SIR), fibrinolysis, and thrombin generation. This agent also inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995) See also: Aprotinin (annotation moved to). Drug Indication For prophylactic use to reduce perioperative blood loss and the need for blood transfusion in patients undergoing cardiopulmonary bypass in the course of coronary artery bypass graft surgery who are at an increased risk for blood loss and blood transfusion. FDA Label Mechanism of Action Aprotinin inhibits serine proteases including trypsin, chymotrypsin and plasmin at a concentration of about 125,000 IU/mL, and kallikrein at 300,000 IU/mL. The inhibition of kallikrein inhibits formation of factor XIIa. This inhibits the intrinsic pathway of coagulation and fibrinolysis. Inhibition of plasmin also slows fibrinolysis. Aprotinin is a broad spectrum protease inhibitor which modulates the systemic inflammatory response (SIR) associated with cardiopulmonary bypass (CPB) surgery. SIR results in the interrelated activation of the hemostatic, fibrinolytic, cellular and humoral inflammatory systems. Aprotinin, through its inhibition of multiple mediators (e.g., kallikrein, plasmin) results in the attenuation of inflammatory responses, fibrinolysis, and thrombin generation. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b). The effects of aprotinin use in ... /cardiopulmonary bypass/ involves a reduction in inflammatory response which translates into a decreased need for allogeneic blood transfusions, reduced bleeding, and decreased mediastinal re-exploration for bleeding. Aprotinin is thought to improve hemostasis during and after cardiopulmonary bypass by preserving platelet membrane receptors that maintain the adhesive and aggregative capacity of platelets. In addition, aprotinin inhibits fibrinolysis through inhibition of plasmin and plasma and tissue kallikreins. Because of its effects on kallikrein, aprotinin also inhibits activation of the intrinsic clotting system (i.e., contact phase of coagulation), a process that both initiates coagulation and promotes fibrinolysis. The relative contribution of these effects of aprotinin to the drug's therapeutic action remains to be fully elucidated. For more Mechanism of Action (Complete) data for APROTININ (6 total), please visit the HSDB record page. |
| Molecular Formula |
C284H432N84O79S7
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|---|---|---|
| Molecular Weight |
6511.51
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| Exact Mass |
6507
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| Elemental Analysis |
C, 52.44; H, 6.59; N, 18.09; O, 19.43; S, 3.45
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| CAS # |
9087-70-1
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| Related CAS # |
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| PubChem CID |
16130295
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| Sequence |
Arg-Pro-Asp-Phe-Cys-Leu-Glu-Pro-Pro-Tyr-Thr-Gly-Pro-Cys-Lys-Ala-Arg-Ile-Ile-Arg-Tyr-Phe-Tyr-Asn-Ala-Lys-Ala-Gly-Leu-Cys-Gln-Thr-Phe-Val-Tyr-Gly-Gly-Cys-Arg-Ala-Lys-Arg-Asn-Asn-Phe-Lys-Ser-Ala-Glu-Asp-Cys-Met-Arg-Thr-Cys-Gly-Gly-Ala(Disulfide bridge: Cys5-Cys55,Cys14-Cys38,Cys30-Cys51)
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| SequenceShortening |
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA(Disulfide bridge: Cys5-Cys55,Cys14-Cys38,Cys30-Cys51)
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| Appearance |
Off-white to light brown solid powder
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| Melting Point |
>100 °C
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| LogP |
-25.4
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| Hydrogen Bond Donor Count |
93
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| Hydrogen Bond Acceptor Count |
97
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| Rotatable Bond Count |
111
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| Heavy Atom Count |
454
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| Complexity |
16700
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| Defined Atom Stereocenter Count |
57
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| SMILES |
NC(=N)NCCC[C@@H](N)C(=O)N1[C@H](CCC1)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CC2=CC=CC=C2)C(=O)N[C@H]3C(=O)N[C@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N4[C@H](CCC4)C(=O)N5[C@@H](CCC5)C(=O)N[C@H](CC6=CC=C(O)C=C6)C(=O)N[C@@H]([C@H](C)O)C(=O)NCC(=O)N7[C@@H](CCC7)C(=O)N[C@H]8C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H]([C@H](C)CC)C(=O)N[C@H](CCCNC(N)=N)C(=O)N[C@@H](CC9=CC=C(O)C=C9)C(=O)N[C@H](CC%10=CC=CC=C%10)C(=O)N[C@@H](CC%11=CC=C(O)C=C%11)C(=O)N[C@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H]%12C(=O)N[C@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](CC%13=CC=CC=C%13)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CC%14=CC=C(O)C=C%14)C(=O)NCC(=O)NCC(=O)N[C@H](CSSC8)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](CC(N)=O)C(=O)N[C@@H](CC%15=CC=CC=C%15)C(=O)N[C@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CSSC%12)C(=O)N[C@@H](CCSC)C(=O)N[C@H](CCCNC(N)=N)C(=O)N[C@@H]([C@H](C)O)C(=O)N[C@@H](CSSC3)C(=O)NCC(=O)NCC(=O)N[C@H](C)C(O)=O
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| InChi Key |
ZPNFWUPYTFPOJU-UHFFFAOYSA-N
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| InChi Code |
InChI=1S/C284H432N84O79S7/c1-21-144(9)222-271(439)337-174(68-46-105-309-282(300)301)239(407)340-187(120-160-77-85-164(374)86-78-160)251(419)341-185(116-156-55-29-24-30-56-156)250(418)342-188(121-161-79-87-165(375)88-80-161)252(420)346-191(123-208(291)378)246(414)322-149(14)230(398)326-168(62-35-39-98-285)234(402)319-146(11)227(395)314-132-215(385)324-181(113-141(3)4)247(415)354-199-137-452-453-138-200-263(431)336-179(97-112-448-20)242(410)331-176(70-48-107-311-284(304)305)244(412)363-226(154(19)372)274(442)358-197(233(401)316-129-212(382)312-130-213(383)318-151(16)278(446)447)135-449-451-139-201(355-253(421)186(117-157-57-31-25-32-58-157)344-256(424)195(127-220(393)394)350-267(435)204-72-50-109-366(204)275(443)167(289)61-43-102-306-279(294)295)265(433)339-182(114-142(5)6)248(416)338-180(93-96-218(389)390)276(444)368-111-52-74-206(368)277(445)367-110-51-73-205(367)268(436)349-189(122-162-81-89-166(376)90-82-162)259(427)362-224(152(17)370)269(437)317-133-216(386)365-108-49-71-203(365)266(434)357-202(264(432)333-169(63-36-40-99-286)235(403)320-148(13)229(397)328-175(69-47-106-310-283(302)303)243(411)360-223(145(10)22-2)272(440)361-222)140-454-450-136-198(325-214(384)131-313-211(381)128-315-232(400)183(119-159-75-83-163(373)84-76-159)351-270(438)221(143(7)8)359-258(426)190(118-158-59-33-26-34-60-158)352-273(441)225(153(18)371)364-245(413)177(335-262(199)430)91-94-207(290)377)261(429)334-172(66-44-103-307-280(296)297)236(404)321-147(12)228(396)327-170(64-37-41-100-287)237(405)330-173(67-45-104-308-281(298)299)238(406)345-192(124-209(292)379)255(423)347-193(125-210(293)380)254(422)343-184(115-155-53-27-23-28-54-155)249(417)332-171(65-38-42-101-288)240(408)353-196(134-369)260(428)323-150(15)231(399)329-178(92-95-217(387)388)241(409)348-194(126-219(391)392)257(425)356-200/h23-34,53-60,75-90,141-154,167-206,221-226,369-376H,21-22,35-52,61-74,91-140,285-289H2,1-20H3,(H2,290,377)(H2,291,378)(H2,292,379)(H2,293,380)(H,312,382)(H,313,381)(H,314,395)(H,315,400)(H,316,401)(H,317,437)(H,318,383)(H,319,402)(H,320,403)(H,321,404)(H,322,414)(H,323,428)(H,324,385)(H,325,384)(H,326,398)(H,327,396)(H,328,397)(H,329,399)(H,330,405)(H,331,410)(H,332,417)(H,333,432)(H,334,429)(H,335,430)(H,336,431)(H,337,439)(H,338,416)(H,339,433)(H,340,407)(H,341,419)(H,342,418)(H,343,422)(H,344,424)(H,345,406)(H,346,420)(H,347,423)(H,348,409)(H,349,436)(H,350,435)(H,351,438)(H,352,441)(H,353,408)(H,354,415)(H,355,421)(H,356,425)(H,357,434)(H,358,442)(H,359,426)(H,360,411)(H,361,440)(H,362,427)(H,363,412)(H,364,413)(H,387,388)(H,389,390)(H,391,392)(H,393,394)(H,446,447)(H4,294,295,306)(H4,296,297,307)(H4,298,299,308)(H4,300,301,309)(H4,302,303,310)(H4,304,305,311)
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| Chemical Name |
4-[[1-[[29a,62a,69,84-tetrakis(4-aminobutyl)-35a,75,78-tris(2-amino-2-oxoethyl)-14a-(3-amino-3-oxopropyl)-8a,41a,72-tribenzyl-50a,53a-di(butan-2-yl)-47a,48,56a,81,90-pentakis(3-carbamimidamidopropyl)-31,60-bis(2-carboxyethyl)-42-[[2-[[2-(1-carboxyethylamino)-2-oxoethyl]amino]-2-oxoethyl]carbamoyl]-57-(carboxymethyl)-11a,13,45-tris(1-hydroxyethyl)-66-(hydroxymethyl)-2a,16,38a,44a-tetrakis[(4-hydroxyphenyl)methyl]-26a,32a,59a,63,87-pentamethyl-20a,34-bis(2-methylpropyl)-51-(2-methylsulfanylethyl)-1a,3,4a,7a,9,10a,12,13a,15,16a,18,19a,22a,24,25a,28a,30,31a,33,34a,36,37a,40a,43a,44,46a,47,49a,50,52a,53,55a,56,58a,59,61a,62,64a,65,68,71,74,77,80,83,86,89,92,95,98-pentacontaoxo-5a-propan-2-yl-39,40,66a,67a,70a,71a-hexathia-a,2,3a,6a,8,9a,11,12a,14,15a,17,18a,21a,23,24a,27a,29,30a,32,33a,35,36a,39a,42a,43,45a,46,48a,49,51a,52,54a,55,57a,58,60a,61,63a,64,67,70,73,76,79,82,85,88,91,94,97-pentacontazahexacyclo[91.71.4.454,117.04,8.019,23.025,29]doheptacontahectan-37-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-[[1-(2-amino-5-carbamimidamidopentanoyl)pyrrolidine-2-carbonyl]amino]-4-oxobutanoic acid
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| Synonyms |
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month Note: Please store this product in a sealed and protected environment, avoid exposure to moisture. |
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| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
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| Solubility (In Vivo) |
Note: Listed below are some common formulations that may be used to formulate products with low water solubility (e.g. < 1 mg/mL), you may test these formulations using a minute amount of products to avoid loss of samples.
Injection Formulations
Injection Formulation 1: DMSO : Tween 80： Saline = 10 : 5 : 85 (i.e. 100 μL DMSO stock solution → 50 μL Tween 80 → 850 μL Saline)(e.g. IP/IV/IM/SC) *Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH ₂ O to obtain a clear solution. Injection Formulation 2: DMSO : PEG300 ：Tween 80 : Saline = 10 : 40 : 5 : 45 (i.e. 100 μL DMSO → 400 μLPEG300 → 50 μL Tween 80 → 450 μL Saline) Injection Formulation 3: DMSO : Corn oil = 10 : 90 (i.e. 100 μL DMSO → 900 μL Corn oil) Example: Take the Injection Formulation 3 (DMSO : Corn oil = 10 : 90) as an example, if 1 mL of 2.5 mg/mL working solution is to be prepared, you can take 100 μL 25 mg/mL DMSO stock solution and add to 900 μL corn oil, mix well to obtain a clear or suspension solution (2.5 mg/mL, ready for use in animals). View More
Injection Formulation 4: DMSO : 20% SBE-β-CD in saline = 10 : 90 [i.e. 100 μL DMSO → 900 μL (20% SBE-β-CD in saline)] Oral Formulations
Oral Formulation 1: Suspend in 0.5% CMC Na (carboxymethylcellulose sodium) Oral Formulation 2: Suspend in 0.5% Carboxymethyl cellulose Example: Take the Oral Formulation 1 (Suspend in 0.5% CMC Na) as an example, if 100 mL of 2.5 mg/mL working solution is to be prepared, you can first prepare 0.5% CMC Na solution by measuring 0.5 g CMC Na and dissolve it in 100 mL ddH2O to obtain a clear solution; then add 250 mg of the product to 100 mL 0.5% CMC Na solution, to make the suspension solution (2.5 mg/mL, ready for use in animals). View More
Oral Formulation 3: Dissolved in PEG400 (Please use freshly prepared in vivo formulations for optimal results.) |
| Preparing Stock Solutions | 1 mg | 5 mg | 10 mg | |
| 1 mM | 0.1536 mL | 0.7679 mL | 1.5357 mL | |
| 5 mM | 0.0307 mL | 0.1536 mL | 0.3071 mL | |
| 10 mM | 0.0154 mL | 0.0768 mL | 0.1536 mL |
*Note: Please select an appropriate solvent for the preparation of stock solution based on your experiment needs. For most products, DMSO can be used for preparing stock solutions (e.g. 5 mM, 10 mM, or 20 mM concentration); some products with high aqueous solubility may be dissolved in water directly. Solubility information is available at the above Solubility Data section. Once the stock solution is prepared, aliquot it to routine usage volumes and store at -20°C or -80°C. Avoid repeated freeze and thaw cycles.
Calculation results
Working concentration： mg/mL；
Method for preparing DMSO stock solution： mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation:：Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O，mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.
| NCT Number | Recruitment | interventions | Conditions | Sponsor/Collaborators | Start Date | Phases |
| NCT00357851 | Completed | Drug: Aprotinin | Pancreatitis | Nemours Children's Clinic | March 2005 | Phase 1 |
| NCT00257751 | Completed | Procedure: Aprotinine | Coronary Artery Disease | Oslo University Hospital | March 2004 | Not Applicable |
| NCT00668031 | Completed | Drug: Trasylol (Aprotinin, BAYA0128) Drug: dolutegravir |
Blood Loss, Surgical | Bayer | February 2005 | Phase 3 |
| NCT00617955 | Completed | Drug: Aprotinin Drug: Amicar |
Cardiac Surgery | State University of New York - Upstate Medical University |
September 2007 | |
| NCT00131040 | Completed | Drug: Aprotinin | Ischemic Heart Disease Angina Pectoris |
Imperial College London | January 2003 | Not Applicable |
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