Aditya Prakash Sarode* and Shraddha Dingare
Solid Phase Peptide Synthesis (SPPS) is a powerful tool for the design and synthesis of peptides with potential antimicrobial activity. In recent years, SPPS has emerged as a promising strategy for the development of new antimicrobial agents. SPPS is a synthetic method that allows for the efficient and rapid production of peptides using solid-phase supports. This technique involves stepwise addition of protected amino acids to a resin-bound peptide chain, followed by deprotection and cleavage to release the desired peptide. The resulting peptides can be modified to enhance their activity, stability, and bioavailability. One of the key advantages of SPPS is its ability to produce peptides with high purity and homogeneity. This is critical for the development of antimicrobial peptides, which require high levels of activity and specificity to target bacterial cells effectively. Additionally, SPPS allows for the production of peptide libraries, which can be screened to identify new antimicrobial agents with improved activity and selectivity. Several studies have demonstrated the effectiveness of SPPS-derived peptides against multidrug-resistant bacteria, including Methicillin-Resistant Staphylococcus aureus (MRSA), Vancomycin-Resistant Enterococcus faecalis (VRE), and Carbapenem-Resistant Klebsiella pneumoniae (CRKP). These peptides have been shown to target bacterial membranes, disrupt cell wall synthesis, and inhibit essential enzymatic processes. In conclusion, SPPS has emerged as a powerful tool for the development of new antimicrobial agents. The ability to rapidly synthesize and modify peptides with high purity and homogeneity has opened up new opportunities for the design of effective therapies against multidrug-resistant bacteria. As the threat of antimicrobial resistance continues to grow, SPPS will play an increasingly important role in the fight against infectious diseases.
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Journal of Antimicrobial Agents received 444 citations as per Google Scholar report