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Cell Shot Nutrition Labs
Welcome to Cell Shot Nutrition Labs, where innovation meets health. Utilizing a combination of rented laboratory space, contract research organizations (CROs), and open-source software, we are dedicated to designing, engineering, and testing solutions that benefit both athletes and the broader community. By exploring the mechanisms of action of peptides and small molecules, we aim to revolutionize supplementation and offer energy options that enhance overall well-being. Join us on our journey to advance human health through cutting research and development.
BPC-157 Predicted to Bind SH3 Domains and Activate Src Family Kinases: In Silico Modeling and Fluorescent Fusion Protein Validation
Abstract
Body Protection Compound-157 (BPC-157) is a synthetic pentadecapeptide derived from human gastric juice with regenerative and cytoprotective effects reported across diverse tissues. Despite extensive preclinical study, the precise molecular mechanism underlying BPC-157's pleiotropic pro-repair effects remains incompletely understood. A key unresolved question is whether BPC-157 acts through extracellular receptor engagement, via intracellular interactions, or through a combination of both. Drawing on preclinical literature, structural modeling, and in silico docking, I propose that BPC-157 adopts a polyproline II helix that engages the Src homology 3 (SH3) domains of Src family kinases (SFKs; c-Src, Yes, Fyn). This interaction relieves SH3 domain-mediated autoinhibition of SFKs, resulting in focal adhesion kinase (FAK)-extracellular signal-regulated kinase (ERK) and phosphoinositide 3-kinase (PI3K)-protein kinase B (Akt) signaling cascades. To enable future experimental validation, a custom baculovirus encoding an engineered mCherry-BPC1572 fusion protein was generated and used to transduce Sf9 cells. Expression of mCherry-BPC1572 was validated by fluorescent imaging and confirmed by western blot at the expected molecular weight (~31 kDa). Collectively, this work proposes a novel structural and functional mechanism for BPC-157, provides in silico docking support, and introduces a molecular tool to probe the BPC-157 interactome.