Cancer and the multi-resistant diseases that plague people today must be controlled to lower mortality rates. With the low susceptibility to resistance, the design and synthesis of peptide assembling was a superior alternative upgrading source for future chemotherapeutic medications. This paradigm first appeared in the pharmaceutical industry. It has been demonstrated that specific peptides exhibit dual functions as antibacterial and anticancer peptides (ACPs). Using a minimalized approach, a 10-residue peptide P1 and Rhodamine tagged peptide P2 were designed and synthesized using solid phase peptide synthesis method (SPPS) for selective activity against microbial and cancer cell lines. Peptide P1 contains RGD sequence has a net charge of +2 and peptide P2 has net charge of -4. The peptide P1 and P2 are characterized by using spectroscopic techniques. Circular dichroism studies showed changes in the secondary structure of peptide 1 and peptide 2 with buffer. Cytotoxicity assay exhibited the viability of normal and cancer cells up to 5 ?g concentrations of peptide 1.Thus, Peptide 1 acts on therapeutic properties like antibacterial and anticancer. Both peptide activities are checked against gram-positive and gram-negative bacteria at lower concentration. We can ensure the toxicity level of designed both peptides. Peptide P1 and peptide P2 sequence are non-toxic and recognition of selective activity against cancer cells.
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