Identification and in silico characterization of a novel peptide inhibitor of angiotensin converting enzyme from pigeon pea (Cajanus cajan).

Background: Plants are important sources of bioactive peptides. Among these, angiotensin converting enzyme (ACE) inhibitory peptides have a major focus on their ability to prevent hypertension. Inhibition of ACE has been established as an effective approach for the treatment of ACE associated diseases.

The allele frequency of T920C mutation in butyrylcholinesterase gene is high in an Indian population.

The genetic variants of butyrylcholinesterase (BChE) are the cause of concern in individuals experiencing prolonged apnea on administration of muscle relaxants. In an Indian community called Vysya, a variant (L307P; T920C) was associated with imperceptible plasma BChE. Since BChE has several pharmacological significances in humans, the identification of its variants having altered activity is very important.

An Indian butyrylcholinesterase variant L307P is not structurally stable: a molecular dynamics simulation study.

The human butyrylcholinesterase (BChE) activity is less than 1% in the serum of silent variant individuals of Vysya community in India. They are homozygous for a point mutation at codon 307 (CTT → CCT) resulting in the substitution of leucine 307 by proline. The reason for the disappearance of the protein in the serum has not been explicated till date.