SARS-CoV-2 – ACE2 peptide library
Angiotensin-converting enzyme 2 (ACE2) is an enzyme involved in the cardiovascular system by decreasing arterial pressure by catalyzing the conversion of angiotensin II to angiotensin (1-7). Angiotensin II is a vasoconstrictor and angiotensin (1-7) is a vasodilatator. This effect makes ACE2 a therapeutic target for cardiovascular disease.
Otherwise, ACE2 also corresponds to a receptor allowing the coronavirus (SARS-CoV-2) to enter the host cell.
Available peptide libraries
Some proteins involved in COVID-19 are identified as leading targets for COVID-19 therapies. sb-PEPTIDE offers two ACE2 peptide libraries :
ACE2 protein – peptide library – Reference #SB048
sb-PEPTIDE provides ACE2 in several peptides of 15 amino acids with an overlap of 11 amino acids.
ACE2 protein – biotinylated peptide library
– Reference #SB048-biotin
The above library is also available with a N-ter biotin of 15 amino acid peptides.
|Peptides length : 15 aa|
|Offset number : 11 aa|
|Amount : 0,5mg or 5*0,5mg (for each peptide)|
|Quality : Crude, 100% LC-MS|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Lyophilized or in solution, in 96-well plate or microtubes|
|Price : Ask for your quote|
|Peptide Solubility Guideline|
1- Jia HP, Look DC, Shi L, et al. J Virol. (2005)
ACE2 receptor expression and severe acute respiratory syndrome coronavirus infection depend on differentiation of human airway epithelia
Studies of patients with severe acute respiratory syndrome (SARS) demonstrate that the respiratory tract is a major site of SARS-coronavirus (CoV) infection and disease morbidity. We studied host-pathogen interactions using native lung tissue and a model of well-differentiated cultures of primary human airway epithelia. Angiotensin converting enzyme 2 (ACE2), the receptor for both the SARS-CoV and the related human respiratory coronavirus NL63, was expressed in human airway epithelia as well as lung parenchyma. As assessed by immunofluorescence staining and membrane biotinylation, ACE2 protein was more abundantly expressed on the apical than the basolateral surface of polarized airway epithelia. Interestingly, ACE2 expression positively correlated with the differentiation state of epithelia. Undifferentiated cells expressing little ACE2 were poorly infected with SARS-CoV, while well-differentiated cells expressing more ACE2 were readily infected. Expression of ACE2 in poorly differentiated epithelia facilitated SARS spike (S) protein-pseudotyped virus entry. Consistent with the expression pattern of ACE2, the entry of SARS-CoV or a lentivirus pseudotyped with SARS-CoV S protein in differentiated epithelia was more efficient when applied to the apical surface. Furthermore, SARS-CoV replicated in polarized epithelia and preferentially exited via the apical surface. The results indicate that infection of human airway epithelia by SARS coronavirus correlates with the state of cell differentiation and ACE2 expression and localization. These findings have implications for understanding disease pathogenesis associated with SARS-CoV and NL63 infections.
2- Hamming I. et al. J Pathol. (2004)
Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis
Severe acute respiratory syndrome (SARS) is an acute infectious disease that spreads mainly via the respiratory route. A distinct coronavirus (SARS-CoV) has been identified as the aetiological agent of SARS. Recently, a metallopeptidase named angiotensin-converting enzyme 2 (ACE2) has been identified as the functional receptor for SARS-CoV. Although ACE2 mRNA is known to be present in virtually all organs, its protein expression is largely unknown. Since identifying the possible route of infection has major implications for understanding the pathogenesis and future treatment strategies for SARS, the present study investigated the localization of ACE2 protein in various human organs (oral and nasal mucosa, nasopharynx, lung, stomach, small intestine, colon, skin, lymph nodes, thymus, bone marrow, spleen, liver, kidney, and brain). The most remarkable finding was the surface expression of ACE2 protein on lung alveolar epithelial cells and enterocytes of the small intestine. Furthermore, ACE2 was present in arterial and venous endothelial cells and arterial smooth muscle cells in all organs studied. In conclusion, ACE2 is abundantly present in humans in the epithelia of the lung and small intestine, which might provide possible routes of entry for the SARS-CoV. This epithelial expression, together with the presence of ACE2 in vascular endothelium, also provides a first step in understanding the pathogenesis of the main SARS disease manifestations.
3- Anguiano L. et al. Curr Med Chem. (2017)
Angiotensin converting enzyme (ACE) 2 is a homologue of ACE that catalyzes the conversion of Angiotensin (Ang) II into Ang1-7, which induces vasodilation, anti-fibrotic, anti-proliferative and anti-inflammatory effects. Given that ACE2 counterbalances the effects of Ang II, it has been proposed as a biomarker in kidney disease patients. Circulating ACE2 has been studied in human and experimental studies under physiological and pathological conditions and different techniques have been assessed to determine its enzymatic activity. In patients with cardiovascular (CV) disease circulating ACE2 has been shown to be increased. In addition, hypertensive and diabetic patients have also shown higher circulating ACE2 activities. A study in type 1 diabetes patients found a negative association between circulating ACE2 and estimated glomerular filtration rate in male and female patients. Recently, it has been demonstrated that circulating ACE2 is increased in male patients with chronic kidney disease (CKD) and that it is independently associated with other classical CV risk factors, such as advanced age and diabetes. Furthermore, circulating ACE2 has been shown to be associated with silent atherosclerosis and CV outcomes in CKD patients. In diabetic nephropathy, experimental studies have demonstrated an increase in circulating ACE2 activity both at early and late stages of the disease, as well as a direct association with increased urinary albumin excretion, suggesting that it may be increased as a renoprotective mechanism in these patients. In this paper we will review the measurement of circulating ACE2 and its role in kidney disease, as well as its potential role as a renal and CV biomarker.