Enzymatic synthesis of peptides has attracted a great deal of attention in recent years. The proteases from bacterial, fungal, plant, and animal sources have been successfully applied to the synthesis of several small peptides, mainly dipeptides and tripeptides. Peptide bonds can be synthesized using proteases in either a thermodynamically controlled or a kinetically controlled manner. The development of new methods suitable for the large-scale production of biologically active peptides has been actively pursued over the last decade due to their bioactive nature as well as better understanding of their biological functions and properties. The aim of this study was to review the basic techniques of peptide synthesis and some advancement in biotechnological methods for their production.

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Drug–polymer conjugation is a simple and efficient approach to synthesizing new, effective, and potent antimicrobial agents to counter the problem of microbial resistance. In the present study, a PEGylated dopamine ester (PDE) was synthesized using the PEGylation process and synthesis of PDE was confirmed by Fourier-transform infrared spectroscopy, elemental analysis (CHNS–O), and atomic force microscopy techniques. Later, the antimicrobial activity of PDE was assessed against four strains of bacteria (Bacillus subtilis, Staphylococcus aureus, Pseudomonas aeruginosa, and Proteus vulgaris; Gram (−)) and two fungi (Aspergillus niger and Aspergillus fumigatus) by the agar well diffusion method. The minimum inhibitory concentration (MIC) of PDE was also determined by the broth dilution method against bacteria. PDE showed significant zones of inhibition ranged from 21 to 27 mm for bacteria and 16 to 20 mm for fungi under study, which were much higher than those for dopamine hydrochloride. MIC values of PDE showed its potential antimicrobial property.

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