BNP

BNP was first discovered in 1988 and has since been recognized as a powerful cardiovascular biomarker . It is a 32-amino acid polypeptide with a ring structure formed by a disulfide bond between two cysteine residues . The recombinant form of BNP, known as recombinant human B-type natriuretic peptide (rhBNP), is produced using recombinant DNA technology and is identical in amino acid sequence to the naturally occurring human BNP .

BNP exerts its effects by binding to natriuretic peptide receptors (NPRs), which are coupled to particulate guanylyl cyclase . This binding leads to an increase in cyclic guanosine monophosphate (cGMP), which in turn activates protein kinase G (PKG) and cyclic nucleotide–coupled phosphodiesterases . These pathways result in vasodilation, natriuresis (excretion of sodium in urine), diuresis (increased urine production), and inhibition of renin and aldosterone secretion .

BNP is widely used as a biomarker for diagnosing and managing heart failure. Elevated levels of BNP in the blood are indicative of heart failure and can help guide treatment decisions . Recombinant human BNP (rhBNP) has been used therapeutically to treat acute decompensated heart failure (ADHF). Studies have shown that rhBNP is effective in improving heart function, reducing plasma BNP levels, and decreasing hospital length of stay in patients with ADHF .

Despite its benefits, the therapeutic efficacy of rhBNP is not always satisfactory, especially in patients with extremely high blood BNP levels . Additionally, there are challenges in developing biosensors for precise monitoring of BNP levels. Future research is focused on overcoming these challenges to improve the clinical utility of BNP and rhBNP .