Snake envenoming is caused by many biological species, rather than a single infectious agent, each with a multiplicity of toxins in their venom. Hence, developing effective treatments is challenging, especially in biodiverse and biogeographically complex countries such as India. The present study represents the first genus-wide proteomics analysis of venom composition across Naja species (N. naja, N. oxiana, and N. kaouthia) found in mainland India. Venom proteomes were consistent between individuals from the same localities in terms of the toxin families present, but not in the relative abundance of those in the venom. There appears to be more compositional variation among N. naja from different locations than among N. kaouthia. Immunoblotting and in vitro neutralization assays indicated cross-reactivity with Indian polyvalent antivenom, in which antibodies raised against N. naja are present. However, we observed ineffective neutralization of PLA₂ activities of N. naja venoms from locations distant from the source of immunizing venoms. Antivenom immunoprofiling by antivenomics revealed differential antigenicity of venoms from N. kaouthia and N. oxiana, and poor reactivity towards 3FTxs and PLA₂s. Moreover, there was considerable variation between antivenoms from different manufacturers. These data indicate that improvements to antivenom manufacturing in India are highly desirable.

Recently, plant protein‐derived peptides with diverse bioactivities have gained special attention with regards to health promoting and disease prevention. Among the different plant sources, edible seeds and nuts are known to contribute essential nutritional needs and promote several health benefits. Storage proteins of edible seeds and nuts are known to fulfill the essential nutritional needs and impart several health promoting benefits. In the present study, we attempt to use in silico approaches to divulge storage proteins derived peptides with angiotensin I‐converting enzyme (ACE)‐inhibition and antioxidant properties. In silico hydrolysis of 10 storage proteins using 8 proteases released multiple peptides exhibiting numerous bioactivities. The storage proteins majorly released ACE inhibitory peptides which were subjected for further evaluation (BIOPEP, PeptideRanker, ToxinPred, AllerTOP, and Pepsite2). A total of 25 peptides were considered potential ACE‐inhibitory peptides. Additionally, AnOxPePred webserver was used to evaluate the potential of storage proteins as precursors of antioxidant peptides. As evident from docking analysis (HPEPDOCK), peptides PGCR, GFEWIAFK, GFFYR, and HFR displayed significant interaction with key residues of Kelch‐like ECH‐associated protein 1, a modulator of intracellular oxidant status. Non‐toxic peptide PGCR exhibited both antioxidant and antihypertensive activities and was found to be the most promising peptide. This study opened new avenue for storage proteins of edible seeds and nuts as ingredients in development of nutraceutical formulations.