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ST

streptokinase (Indikinase)

✓ Approved

Unichem · PLG · Recombinant Proteins

What is streptokinase?

streptokinase is a recombinant proteins developed by Unichem. It is approved for therapeutic indications via injectable (others) or intravenous (iv).

Drug Profile

Brand NamesIndikinase
CompanyUnichem
Drug ClassRecombinant Proteins
Molecular TargetPLG
RouteInjectable (Others), Intravenous (IV)
StatusApproved
Sources: ClinicalTrials.gov, Unichem

Mechanism of Action

Molecular Targets

streptokinase acts on 1 molecular target:

PLGplasminogen (HAE4)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

streptokinase is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Cardiac disordersMyocardial infarction✓ Approved

Related Research Articles

PubMedThe Journal of infection2026-10-19

Human Antibody Responses to Group A Streptococcus Infection: A Systematic Review.

Barr Rachael R, Frost Hannah H, Abo Yara-Natalie YN, Tucker Faye F et al.

Group A Streptococcus (GAS) is a leading global cause of infectious disease morbidity and mortality. A major barrier to GAS vaccine development is our incomplete understanding of human immunity. We undertook, to our knowledge, the first systematic review describing human antibody responses following GAS infection. Eligible studies were publications reporting human antibody responses to any GAS antigen in individuals with microbiologically confirmed GAS infection. Case reports and studies primarily describing post-streptococcal autoimmune complications were excluded. Databases were last searched on 15th November 2025. Risk of bias was assessed using the relevant tools from the Joanna Briggs Institute. Results are presented in narrative form as meta-analysis was not appropriate. A total of 143 studies spanning 1948-2025 met inclusion criteria. Most studies (83%) were conducted in the Global North and focused on tonsillopharyngitis (79·4%). Antibody responses were measured in serum (99·3%) and/or saliva (2·1%), targeting 116 distinct GAS antigens. The proportion of individuals exhibiting an antibody response to five antigens (SLO, DNase B, GAC, M protein and Streptokinase) was significantly greater in cases when compared with healthy controls. In longitudinal studies, the peak antibody titres were detected at a median of 28 days post-infection. Higher pre-infection titres of some antibodies (M protein, SpyCEP, SpyAD, SLO, DNase B, SpnA, T25, K4S2) correlated with subsequent protection from GAS infection or reduced severity of disease in three separate studies. Heterogeneity across studies prevented clear conclusions regarding how post-infection antibody responses vary by GAS serotype, participant age, infection site, or disease severity. This review synthesizes 77 years of heterogenous studies describing antibody responses to GAS infection. Limitations of this review arise from the heterogeneity between studies and study risk of bias. Despite this, we identify major gaps in our understanding of the magnitude, kinetics, and protective role of antibody responses. Our synthesis uncovers information that will support GAS vaccine development including: guidance on sampling time points and the identification of antibodies that may be associated with protection from disease, as well as the need for standardisation of laboratory methodology and minimally-biased antigen discovery approaches.

PMID 42896813
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PubMedAdvanced healthcare materials2026-10-16

Translating Stroke Microenvironment Cues Into Materials Design: Intelligent Nanomaterials for Ischemic Stroke Therapy.

Chen Jiajun J, Li Xiangqi X, Deng Jiali J, Wang Ying Y et al.

Ischemic stroke (IS), caused by cerebral blood vessel occlusion, leads to ischemia, hypoxia, and irreversible brain tissue damage. Current treatments primarily rely on thrombolytic agents like alteplase, urokinase, and streptokinase for rapid reperfusion. However, these therapies are limited by narrow therapeutic windows, rapid clearance, poor blood-brain barrier (BBB) penetration, off-target effects, and the complex ischemic microenvironment. These have led to increased interest in nanomaterial-based platforms to improve the precision and efficacy of IS treatment. The IS microenvironment, characterized by oxidative stress, inflammation, ionic imbalance, acidosis, and BBB disruption, provides valuable cues for designing responsive nanomaterials. Nanomaterials engineered to respond to reactive oxygen species, pH, enzymes, light, ultrasound, or magnetic fields can enable targeted drug delivery, controlled release, and multi-modal interventions, enhancing therapeutic precision. This review discusses the IS microenvironment, limitations of traditional therapies, recent advances in intelligent nanomaterials for IS treatment, and the major barriers that currently limit clinical translation.

PMID 42885941
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PubMedPakistan journal of medical sciences2026-10-01

Outcomes of thrombolytic therapy in prosthetic valve thrombosis; a single centre study.

Rana Ikram Ahmed IA, Munawar Fatina F, Mubasher Ayesha A, Talha Bajwa Muhammad M

To determine the outcomes of thrombolytic therapy in prosthetic valve thrombosis. Data was taken from the hospital discharge database, of the Tahir Heart Institute, for patients admitted from January 01, 2016 to June 30, 2024. Definitive diagnosis was made with transthoracic echocardiography showing an obstructed prosthetic valve for patients presenting with new-onset dyspnea. Streptokinase infusion was given per ACC/AHA guidelines with twelve-hourly TTE for transvalvular gradient assessment. The primary outcome was successful thrombolysis with reduction in transvalvular gradients. Data was analyzed by Microsoft Excel. Patients were followed up over time. Approximately 0.1% of total hospital admissions, i.e. twenty-seven cases, were found to have prosthetic valve thrombosis. Target gradients on TTE were achieved for 71% (n=17) of mitral and 100% (n=3) of aortic valves: thrombolysis was successful in 74% (n=20), partial success in 18.5% (n=5) and unsuccessful in 7.4% (n=2) of cases. Subsequent complications were: myocardial infarction 7.4% (n=2), embolic phenomena 14.8 % (n=4), coronary emboli 7.4% (n=2), brain emboli 7.4% (n=2), re-thromboses 7.4% (n=2) and in-hospital mortality 7.4% (n=2) of cases. The mean time for follow-up after discharge was 3.04 ± 2.07 years; one patient died a year after discharge. Thrombolytic therapy with streptokinase has been shown to be an effective and relatively safe method for managing prosthetic valve thrombosis.

PMID 42819587
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PubMedHuman immunology2026-09-29

Rational truncation of streptokinase reduces immunogenicity while preserving plasminogen activation: in vitro and in vivo analysis.

Gunasekaran Vijay V, Suthakaran Pichaimuthu P, Namasivayam Vigneshwaran V, Ponnusami V V

The clinical utility of streptokinase, a widely used and cost-effective thrombolytic agent, has gained importance post COVID-19 due to increase in cardiovascular diseases globally. But the strong humoral immunogenicity exhibited by it, restricts its usage. Building upon our prior work of developing truncated streptokinase variants and their plasminogen activation study, we report here the results of immunogenicity studies for identification of variants with reduced immunogenicity. A panel of ten rationally truncated and recombinantly expressed streptokinase fragments were screened for antibody recognition and immunogenicity potential. Out of the ten fragments, two N-terminal constructs (amino acid residues 1-300 and 1-173) exhibited approximately 40-45% lower ELISA immunoreactivity compared with full-length streptokinase during initial in vitro screening. These fragments were also already reported to retain >85% of native plasminogen activation activity. In vivo evaluation of the fragments in rabbits demonstrated significantly attenuated humoral responses over a 28-day immunization period, confirmed by longitudinal antibody titration and cumulative area-under-the-curve analysis when compared to the full-length streptokinase. Fragment 1-173 emerged as a promising lower-immunogenic thrombolytic candidate, and this work demonstrates that rational domain minimization can decouple functional competence from immunodominant regions in streptokinase establishing a broadly applicable framework for engineering improved therapeutic proteins.

PMID 42810275
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PubMedJournal of structural biology2026-09-24

In silico engineering fibrin-directed streptokinase - kringle 2 fusion: Structural insights into fibrin interaction and plasminogen recognition.

Mohammed Rawaa Kh RK, Buniya Harith K HK

Streptokinase (SK) is an effective plasminogen-activating fibrinolytic protein, but its lack of intrinsic fibrin specificity limits thrombus-directed fibrinolysis. We computationally evaluated an engineered SK-K2 fusion in which the fibrin-interacting Kringle 2 (K2) domain of human tissue-type plasminogen activator was appended to the SK C-terminus. Structural modeling showed high K2 confidence (mean pLDDT = 85.67), and all 22 K2 residues at the predicted fibrin interface had pLDDT values ≥70 (mean = 89.88). HDOCK ranked SK-K2-fibrin more favorably than native SK-fibrin (-276.71 vs. -249.24), while PRODIGY predicted a more favorable binding free energy (-14.9 vs. -13.3 kcal/mol). Although native SK showed a more favorable HDOCK score toward plasminogen, both plasminogen complexes had identical PRODIGY-predicted binding free energies (-11.2 kcal/mol) and closely comparable dissociation constants, indicating no marked computational loss in predicted plasminogen-binding characteristics after K2 fusion. PDBePISA showed direct K2 participation and a larger chain-matched fibrin interface for SK-K2 than native SK, with six hydrogen bonds and an Asp291-Arg515 salt bridge (2.966 Å) in the HDOCK-derived complex. An independent MOE workflow reproduced the fibrin-directed ranking, with SK-K2 showing a more favorable S score than native SK (-101.8501 vs. -93.9472). PDBePISA analysis of the independent MOE complex identified Arg515 in a second salt bridge, Arg515-Glu220 (3.369 Å), providing residue-level convergence across both docking models. These findings support the structural rationale for C-terminal K2 engineering of SK and prioritize SK-K2, particularly Arg515, for experimental evaluation of fibrin association, plasminogen activation, and clot-directed fibrinolysis.

PMID 42785651
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PubMedActa cirurgica brasileira2026-09-17

Evaluation of polymeric films and streptokinase for prevention of postoperative intra-abdominal adhesion in rabbits.

Teixeira Luisa Gouvêa LG, Brito Helena Cristina Delgado HCD, Teixeira Bruna Nunes BN, Barata Julielton de Souza JS et al.

To evaluate the effectiveness of polymer-based strategies for preventing intra-abdominal adhesions after small colon enterotomy and enterorrhaphy in a rabbit experimental model. Twenty-four female New Zealand White rabbits were randomly allocated into four groups (n = 6): film composed of a blend of sodium carboxymethylcellulose and polyvinyl alcohol (NaCMC-PVA); NaCMC-PVA-streptokinase (STP) film; intra-abdominal STP infusion; and no treatment. Hematological parameters were assessed preoperatively and at three and seven days postoperatively. Macroscopic evaluation of intra-abdominal adhesions and histopathological analysis of the enterorrhaphy site were performed on postoperative day 7. Results were compared within and between experimental groups. Treated groups exhibited fewer hematological alterations compared with the control group. No statistically significant differences were observed among groups regarding adhesion severity or histopathological scores (p> 0.05). The NaCMC-PVA film showed the lowest absolute incidence of adhesions and did not impair intestinal remesothelialization. Based on the biological findings from this study, the NaCMC-PVA film exhibited acceptable handling characteristics and biological compatibility. These findings suggest its potential as a mechanical barrier for preventing abdominal adhesion. However, further studies with larger sample sizes and longer follow-up periods are required to confirm its effectiveness.

PMID 42752722
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