MedKoo Cat#: 414208 | Name: Aprotinin
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Description:

WARNING: This product is for research use only, not for human or veterinary use.

Aprotinin is a small protein bovine pancreatic trypsin inhibitor, or basic trypsin inhibitor of bovine pancreas, which is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes.

Chemical Structure

Aprotinin
CAS#9087-70-1

Theoretical Analysis

MedKoo Cat#: 414208

Name: Aprotinin

CAS#: 9087-70-1

Chemical Formula: C284H425N84O79S7

Exact Mass: 6499.9866

Molecular Weight: 6504.45

Elemental Analysis: C, 52.44; H, 6.59; N, 18.09; O, 19.43; S, 3.45

Price and Availability

Size Price Availability Quantity
10mg USD 250.00 2 Weeks
25mg USD 450.00 2 Weeks
50mg USD 750.00 2 Weeks
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Synonym
Aprotinin; HSDB7502; HSDB-7502; HSDB 7502; RP9921; RP-9921; RP 9921; Bovine Pancreatic Trypsin Inhibitor; BPTI
IUPAC/Chemical Name
L-Arginyl-L-prolyl-L-aspartyl-L-phenylalanyl-L-cysteinyl-L-leucyl-L-glutamyl-L-prolyl-L-prolyl-L-tyrosyl-L-threonylglycyl-L-prolyl-L-cysteinyl-L-lysyl-L-alanyl-L-arginyl-L-isoleucyl-L-isoleucyl-L-arginyl-L-tyrosyl-L-phenylalanyl-L-tyrosyl-L-asparaginyl-L-alanyl-L-lysyl-L-alanylglycyl-L-leucyl-L-cysteinyl-L-glutaminyl-L-threonyl-L-phenylalanyl-L-valyl-L-tyrosylglycylglycyl-L-cysteinyl-L-arginyl-L-alanyl-L-lysyl-L-arginyl-L-asparaginyl-L-asparaginyl-L-phenylalanyl-L-lysyl-L-seryl-L-alanyl-L-glutamyl-L-aspartyl-L-cysteinyl-L-methionyl-L-arginyl-L-threonyl-L-cysteinylglycylglycyl-L-alanine cyclic (5-55), (14-38), (30-51) tris(disulfide)
InChi Key
ZPNFWUPYTFPOJU-LPYSRVMUSA-N
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)/t144-,145-,146-,147-,148-,149-,150-,151-,152+,153+,154+,167-,168-,169-,170-,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-,221-,222-,223-,224-,225-,226-/m0/s1
SMILES Code
ccc([C@@H]1NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H]2CSSC[C@@H]3NC(CNC(CNC(C(NC(C(C(C)C)NC(C(NC([C@H]([C@H](O)C)NC(C(NC([C@@H](NC([C@@H](NC(CNC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@H]([C@H](CC)C)NC1=O)=O)CCCNC(N)=N)=O)Cc4ccc(O)cc4)=O)Cc5ccccc5)=O)Cc6ccc(O)cc6)=O)CC(N)=O)=O)C)=O)CCCCN)=O)C)=O)=O)CC(C)C)=O)CSSC[C@@H](C(NC(C(NC(C(N[C@H](C(NC(C(NCC(NCC(N[C@H](C(O)=O)C)=O)=O)=O)CSSCC(C(NC(C(NC(C(N7CCCC7C(N8CCCC8C(NC(C(N[C@H](C(NCC(N9CCCC9C(N2)=O)=O)=O)[C@H](O)C)=O)Cc%10ccc(O)cc%10)=O)=O)=O)CCC(O)=O)=O)Cc(c)c)=O)NC([C@@H](NC([C@@H](NC([C@@H]%11CCCN%11C([C@H](CCCNC(N)=N)N)=O)=O)CC(O)=O)=O)Cc%12ccccc%12)=O)=O)[C@H](O)C)=O)CCCNC(N)=N)=O)CCSC)=O)NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC3=O)CCCNC(N)=N)=O)C)=O)CCCCN)=O)CCCNC(N)=N)=O)CC(N)=O)=O)CC(N)=O)=O)Cc%13ccccc%13)=O)CCCCN)=O)CO)=O)C)=O)CCC(O)=O)=O)CC(O)=O)=O)=O)CCC(N)=O)=O)=O)Cc%14ccccc%14)=O)=O)Cc%15ccc(O)cc%15)=O)=O)=O)=O)CCCCN)=O)C)=O)CCCNC(N)=N)=O)c
Appearance
Solid powder
Purity
Refer to the Certificate of Analysis
Shipping Condition
Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs.
Storage Condition
Dry, dark and at 0 - 4 C for short term (days to weeks) or -20 C for long term (months to years).
Solubility
To be determined
Shelf Life
>2 years if stored properly
Drug Formulation
To be determined
Stock Solution Storage
0 - 4 C for short term (days to weeks), or -20 C for long term (months).
HS Tariff Code
2934.99.9001
More Info
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).
Product Data
Biological target:
Aprotinin is a bovine pancreatic trypsin inhibitor (BPTI) inhibitor which inhibits trypsin and chymotrypsin with Kis of 0.06 pM and 9 nM, respectively.
In vitro activity:
Treatment with different concentrations of aprotinin significantly decreased the surviving fraction and inhibited the growth of both normal and BC cell lines (p < 0.001) tested in this study (Table 1). Higher doses of aprotinin treatment were associated with a correspondingly further drop in the percentage of survival fraction (Fig. 1). The majority of growth inhibitory effects was achieved by the application of 1 TIU/mL of aprotinin. Compared to tumor cell lines, normal fibroblast cell line HDF-1 showed less sensitivity to growth inhibitory effects of aprotinin at 0.4 TIU/mL (p < 0.001), 0.7 TIU/mL (p = 0.003) and 1.5 TIU/mL (p = 0.02) concentrations of aprotinin. Compared to other BC cell lines, MCF-7 cell line showed higher sensitivity to growth inhibitory effects of aprotinin at a concentration of 0.4 TIU/mL (p < 0.001). Reference: Adv Clin Exp Med. 2019 Feb;28(2):151-157. https://pubmed.ncbi.nlm.nih.gov/30411549/
In vivo activity:
To investigate the effect of aprotinin on ENaC-mediated sodium conservation, we studied mice on a sodium-replete and low-sodium diet for 9 days in the metabolic cages. As shown in Fig. 2a, urinary sodium excretion was not affected by aprotinin over 9 days under a sodium-replete diet. Food and fluid intake as well as urine volume were similar in all groups (Supplementary Fig. S2a–c). Under a low-sodium diet, placebo-treated mice lowered urinary sodium excretion within 2 days and remained constant thereafter. In contrast, sodium conservation was impaired in aprotinin-treated mice during the first 5 days (Fig. 2a). Body weight dropped transiently in placebo- and aprotinin-treated mice under a control diet during the first days in the metabolic cages and stabilized thereafter (Fig. 2b). Body weight loss was pronounced under a low-sodium diet in placebo-treated mice and stabilized at the end of the study period. In contrast, aprotinin-treated mice under a low-sodium diet experienced enhanced bw loss that reached a new steady state at a lower level. Reference: Acta Pharmacol Sin. 2021 Mar 23. https://pubmed.ncbi.nlm.nih.gov/33758357/
Solvent mg/mL mM comments
Solubility
Water 100.0 15.37
Note: There can be variations in solubility for the same chemical from different vendors or different batches from the same vendor. The following factors can affect the solubility of the same chemical: solvent used for crystallization, residual solvent content, polymorphism, salt versus free form, degree of hydration, solvent temperature. Please use the solubility data as a reference only. Warming and sonication will facilitate dissolving. Still have questions? Please contact our Technical Support scientists.

Preparing Stock Solutions

The following data is based on the product molecular weight 6,504.45 Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.

Recalculate based on batch purity %
Concentration / Solvent Volume / Mass 1 mg 5 mg 10 mg
1 mM 1.15 mL 5.76 mL 11.51 mL
5 mM 0.23 mL 1.15 mL 2.3 mL
10 mM 0.12 mL 0.58 mL 1.15 mL
50 mM 0.02 mL 0.12 mL 0.23 mL
Formulation protocol:
1. Bojkova D, Bechtel M, McLaughlin KM, McGreig JE, Klann K, Bellinghausen C, Rohde G, Jonigk D, Braubach P, Ciesek S, Münch C, Wass MN, Michaelis M, Cinatl J Jr. Aprotinin Inhibits SARS-CoV-2 Replication. Cells. 2020 Oct 30;9(11):2377. doi: 10.3390/cells9112377. PMID: 33143316; PMCID: PMC7692688. 2. Soleyman-Jahi S, Sadeghi F, Afshari Z, Barati T, Ghasemi S, Muhammadnejad S, Amanpour S, Zendehdel K. Anti-neoplastic effects of aprotinin on human breast cancer cell lines: In vitro study. Adv Clin Exp Med. 2019 Feb;28(2):151-157. doi: 10.17219/acem/89770. PMID: 30411549. 3. Song EJ, Españo E, Shim SM, Nam JH, Kim J, Lee K, Park SK, Lee CK, Kim JK. Inhibitory effects of aprotinin on influenza A and B viruses in vitro and in vivo. Sci Rep. 2021 May 3;11(1):9427. doi: 10.1038/s41598-021-88886-1. PMID: 33941825; PMCID: PMC8093218. 4. Wörner S, Bohnert BN, Wörn M, Xiao M, Janessa A, Birkenfeld AL, Amann K, Daniel C, Artunc F. Renal effects of the serine protease inhibitor aprotinin in healthy conscious mice. Acta Pharmacol Sin. 2021 Mar 23. doi: 10.1038/s41401-021-00628-1. Epub ahead of print. PMID: 33758357.
In vitro protocol:
1. Bojkova D, Bechtel M, McLaughlin KM, McGreig JE, Klann K, Bellinghausen C, Rohde G, Jonigk D, Braubach P, Ciesek S, Münch C, Wass MN, Michaelis M, Cinatl J Jr. Aprotinin Inhibits SARS-CoV-2 Replication. Cells. 2020 Oct 30;9(11):2377. doi: 10.3390/cells9112377. PMID: 33143316; PMCID: PMC7692688. 2. Soleyman-Jahi S, Sadeghi F, Afshari Z, Barati T, Ghasemi S, Muhammadnejad S, Amanpour S, Zendehdel K. Anti-neoplastic effects of aprotinin on human breast cancer cell lines: In vitro study. Adv Clin Exp Med. 2019 Feb;28(2):151-157. doi: 10.17219/acem/89770. PMID: 30411549.
In vivo protocol:
1. Song EJ, Españo E, Shim SM, Nam JH, Kim J, Lee K, Park SK, Lee CK, Kim JK. Inhibitory effects of aprotinin on influenza A and B viruses in vitro and in vivo. Sci Rep. 2021 May 3;11(1):9427. doi: 10.1038/s41598-021-88886-1. PMID: 33941825; PMCID: PMC8093218. 2. Wörner S, Bohnert BN, Wörn M, Xiao M, Janessa A, Birkenfeld AL, Amann K, Daniel C, Artunc F. Renal effects of the serine protease inhibitor aprotinin in healthy conscious mice. Acta Pharmacol Sin. 2021 Mar 23. doi: 10.1038/s41401-021-00628-1. Epub ahead of print. PMID: 33758357.
1: Robert S, Wagner BK, Boulanger M, Richer M. Aprotinin. Ann Pharmacother. 1996 Apr;30(4):372-80. doi: 10.1177/106002809603000410. PMID: 8729892. 2: Alston TA. Aprotinin. Int Anesthesiol Clin. 2004 Fall;42(4):81-91. doi: 10.1097/00004311-200404240-00009. PMID: 15577702. 3: Westaby S. Aprotinin in perspective. Ann Thorac Surg. 1993 Apr;55(4):1033-41. doi: 10.1016/0003-4975(93)90149-c. PMID: 7682054. 4: Dietrich W. Aprotinin: 1 year on. Curr Opin Anaesthesiol. 2009 Feb;22(1):121-7. doi: 10.1097/ACO.0b013e32831c833f. PMID: 19295302. 5: Sodha NR, Boodhwani M, Bianchi C, Ramlawi B, Sellke FW. Aprotinin in cardiac surgery. Expert Rev Cardiovasc Ther. 2006 Mar;4(2):151-60. doi: 10.1586/14779072.4.2.151. PMID: 16509811. 6: Royston D. The current place of aprotinin in the management of bleeding. Anaesthesia. 2015 Jan;70 Suppl 1:46-9, e17. doi: 10.1111/anae.12907. PMID: 25440394. 7: Royston D. Aprotinin therapy. Br J Anaesth. 1994 Dec;73(6):734-7. doi: 10.1093/bja/73.6.734. PMID: 7533511. 8: Davis R, Whittington R. Aprotinin. A review of its pharmacology and therapeutic efficacy in reducing blood loss associated with cardiac surgery. Drugs. 1995 Jun;49(6):954-83. doi: 10.2165/00003495-199549060-00008. PMID: 7543841. 9: Peters DC, Noble S. Aprotinin: an update of its pharmacology and therapeutic use in open heart surgery and coronary artery bypass surgery. Drugs. 1999 Feb;57(2):233-60. doi: 10.2165/00003495-199957020-00015. PMID: 10188764. 10: McEvoy MD, Reeves ST, Reves JG, Spinale FG. Aprotinin in cardiac surgery: a review of conventional and novel mechanisms of action. Anesth Analg. 2007 Oct;105(4):949-62. doi: 10.1213/01.ane.0000281936.04102.9f. PMID: 17898372. 11: Fussi F. Aprotinin: mechanism of action and therapeutical uses. Boll Chim Farm. 1980 Nov;119(11):631-46. PMID: 6164378. 12: Royston D, van Haaften N, De Vooght P. Aprotinin; friend or foe? A review of recent medical literature. Eur J Anaesthesiol. 2007 Jan;24(1):6-14. doi: 10.1017/S0265021506001955. Epub 2006 Nov 14. PMID: 17105674. 13: Donahue MA, Price PM. Aprotinin: antifibrinolytic and anti-inflammatory mechanisms of action in cardiac surgery with cardiopulmonary bypass. Dynamics. 2002 Fall;13(3):16-23. PMID: 12640841. 14: Kristeller JL, Roslund BP, Stahl RF. Benefits and risks of aprotinin use during cardiac surgery. Pharmacotherapy. 2008 Jan;28(1):112-24. doi: 10.1592/phco.28.1.112. PMID: 18154481. 15: Schisano G, Nina P. Aprotinin and hemostasis. J Neurosurg. 2005 Apr;102(4):757-8; author reply 758. doi: 10.3171/jns.2005.102.4.0757. PMID: 15871522. 16: Royston D. The serine antiprotease aprotinin (Trasylol): a novel approach to reducing postoperative bleeding. Blood Coagul Fibrinolysis. 1990 Mar- Apr;1(1):55-69. PMID: 1715200. 17: Royston D, De Hert S, van der Linden J, Ouattara A, Zacharowski K. A special article following the relicence of aprotinin injection in Europe. Anaesth Crit Care Pain Med. 2017 Apr;36(2):97-102. doi: 10.1016/j.accpm.2017.02.001. Epub 2017 Feb 13. PMID: 28215980. 18: Dobkowski WB, Murkin JM. A risk-benefit assessment of aprotinin in cardiac surgical procedures. Drug Saf. 1998 Jan;18(1):21-41. doi: 10.2165/00002018-199818010-00003. PMID: 9466086. 19: Kokoszka A, Kuflik P, Bitan F, Casden A, Neuwirth M. Evidence-based review of the role of aprotinin in blood conservation during orthopaedic surgery. J Bone Joint Surg Am. 2005 May;87(5):1129-36. doi: 10.2106/JBJS.D.02240. PMID: 15866981. 20: Smith PK, Shah AS. The role of aprotinin in a blood-conservation program. J Cardiothorac Vasc Anesth. 2004 Aug;18(4 Suppl):24S-28S. doi: 10.1053/j.jvca.2004.02.001. PMID: 15368202.