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

CAP37, a protein constitutively EXPRESSED in human neutrophils and induced in responseto infection in corneal epithelial cells, plays a significant role in host defense against infection. Initiallyidentified through its potent bactericidal activity for Gram-negative bacteria, it is now known that CAP37regulates numerous host cell functions, including corneal epithelial cell chemotaxis. Delineation of thedomains of CAP37 that define these functions and synthesize bioactive peptides for therapeutic use have alsobeen 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-mimicchemo-structure by connecting conserved fragments based on the neutrophil immune defense CAP37 proteinas an in-silico antibacterial and wound-healing canditate agent. This in silico effort was accomplished byutilizing various generated descriptors of proteins, compounds and their interactions resulting in aperformance/cost evaluation study for a GPU-based drug discovery application on volunteer computingapproaches based on Automated Structure-Activity Relationship Minings in Connecting Chemical Structureto Biological Profiles for the generation of novel Computational biomodeling of 3D drug-protein binding freeenergy evaluation

Rational Elaborated Common Strategies Employed For The Efficient in Silico Optimization Of An Accesible Synthetically (AMPs) Peptidomimetic-similar To An Amphiphile-Based Pharmacophoric Agent As A Promising Enhanced Therapeutic Antimicrobial Agent

Antimicrobial peptides (AMPs) which predominantly act via membrane active mechanisms haveemerged as an exciting class of antimicrobial agents with tremendous potential to overcome the globalepidemic of antibiotics-resistant infections. The first generation of AMPs derived from natural sources asdiverse as plants, insects and humans has provided a wealth of compositional and structural information todesign novel synthetic AMPs with enhanced antimicrobial potencies and selectivities, reduced cost ofproduction due to shorter sequences and improved stabilities under physiological conditions. As a rationalresult we discovered for the first time the GENEA-Antimamphiler-109 utilizing threading/structure-basedBIOGENETOLIGANDOROLTM Rational Strategies employed for the in silico design and optimization ofsynthetic antimicrobial peptide mimic amphiphile-based pharmacophoric agents with promising enhancedtherapeutic potentials introducing the iview: an interactive WebGL visualizer for protein-ligand complexthrough a subpocket analysis method for fragment-based drug discovery through a KNIME-SharedBiogenetoligandorolTM binding site amino acid predicted similarity subpockets