Nesiritide (Natrecor): A Comprehensive Monograph on a Controversial Cardiovascular Agent

Section 1: Profile of a Recombinant Natriuretic Peptide

1.1. Identification and Chemical Structure

Nesiritide is a synthetically produced, purified preparation of human B-type natriuretic peptide (hBNP), a hormone endogenously produced by the ventricular myocardium in response to increased wall stress and volume overload.[1] It is classified as a biotech drug, manufactured using recombinant DNA technology with an

Escherichia coli host system.[2] As a therapeutic agent, Nesiritide is identical in its amino acid composition to the native human peptide, designed to replicate its physiological functions in a clinical setting.[2]

The peptide consists of a single chain of 32 amino acids.[1] Its structure is characterized by a 17-amino acid ring formed by an intramolecular disulfide bond between the cysteine residues at positions 10 and 26.[6] This ring structure is a conserved feature across the family of natriuretic peptides and is crucial for receptor binding and biological activity. The full amino acid sequence of Nesiritide is: Ser-Pro-Lys-Met-Val-Gln-Gly-Ser-Gly-Cys-Phe-Gly-Arg-Lys-Met-Asp-Arg-Ile-Ser-Ser-Ser-Ser-Gly-Leu-Gly-Cys-Lys-Val-Leu-Arg-Arg-His.[5]

For clinical use, Nesiritide is formulated as a citrate salt and supplied as a sterile, white to off-white lyophilized powder that requires reconstitution before intravenous administration.[2] Its fundamental chemical and physical properties are well-defined, with a chemical formula of

C143​H244​N50​O42​S4​ and a molecular weight of approximately 3464.0 g/mol.[1] The drug has been assigned numerous identifiers across various chemical and pharmacological databases, ensuring its unambiguous identification for research, clinical, and regulatory purposes.

Table 1: Key Identifiers and Properties of Nesiritide