High-dimension profiling data generate a multifunctional peptide-mimic chemo-structure by connecting conserved fragments based on the neutrophil immune defense CAP37 protein as an in-silico antibacterial and woundhealing candidate agent

Abstract

CAP37, a protein constitutively EXPRESSED in human neutrophils and induced in response
to infection in corneal epithelial cells, plays a significant role in host defense against infection. Initially
identified through its potent bactericidal activity for Gram-negative bacteria, it is now known that CAP37
regulates numerous host cell functions, including corneal epithelial cell chemotaxis. Delineation of the
domains of CAP37 that define these functions and synthesize bioactive peptides for therapeutic use have also
been explored. Novel findings of a multifunctional domain between a 120 and 146 have also been reported.
Here, in Biogenea Pharmaceuticals Ltd we for the first time generated a multifunctional peptide-mimic
chemo-structure by connecting conserved fragments based on the neutrophil immune defense CAP37 protein
as an in-silico antibacterial and wound-healing canditate agent. This in silico effort was accomplished by
utilizing various generated descriptors of proteins, compounds and their interactions resulting in a
performance/cost evaluation study for a GPU-based drug discovery application on volunteer computing
approaches based on Automated Structure-Activity Relationship Minings in Connecting Chemical Structure
to Biological Profiles for the generation of novel Computational biomodeling of 3D drug-protein binding free
energy evaluation.