• Dr. Ramesha Baba, A
• Nagendra Chowdary
• Dr. Umashankara. M
• Dr. Niranjan Raj. S

In this study we mainly focus on structure-activity relationship aspects and important physiochemical properties that influence the antimicrobial and toxic properties of five hybrid peptides having one γ/β aminoacid. The contributions of individual amino acids with respect to the position in displaying antibacterial properties are presented. The mechanism of action of different peptides towards antimicrobial activity is also studied using SEM. The current study enhances knowledge on design strategies to illustrate the importance of antimicrobial peptide research in the development of next-generation antibiotics.

Antimicrobial peptides; Mechanism of action; Hybrid peptides; γ- aminoacid; β- aminoacid; Scanning Electron Microscopy(SEM)

"Design of hydrophobic hybrid tri peptides as broad spectrum potent antimicrobial agents with enhanced cell selectivity", International Journal of Emerging Technologies and Innovative Research (www.jetir.org), ISSN:2349-5162, Vol.5, Issue 12, page no.211-220, December-2018, Available :http://www.jetir.org/papers/JETIR1812632.pdf

"Design of hydrophobic hybrid tri peptides as broad spectrum potent antimicrobial agents with enhanced cell selectivity", International Journal of Emerging Technologies and Innovative Research (www.jetir.org | UGC and issn Approved), ISSN:2349-5162, Vol.5, Issue 12, page no. pp211-220, December-2018, Available at : http://www.jetir.org/papers/JETIR1812632.pdf