Molecular Modification of Kex2 P1' Site Enhances Expression and Druggability of Fungal Defensin.

ABSTRACT: Pichia pastoris is the widely used expression system for producing recombinant secretory proteins. It is known that Kex2 protease plays a vital role in the process of protein secretion, in which the P1' site affects its cleavage efficiency. To enhance the expression level of fungal defensin-derived peptide NZ2114, this work attempts to optimize the P1' site of Kex2 by replacing it with 20 amino acids in turn. The results showed that when the amino acid of the P1' site was changed to Phe (F), the yield of target peptide significantly increased from 2.39 g/L to 4.81 g/L. Additionally, the novel peptide F-NZ2114 (short for FNZ) showed strong antimicrobial activity against Gram-positive (G⁺) bacteria, especially for Staphylococcus aureus and Streptococcus agalactiae

SUBMITTER: Jin Y 

PROVIDER: S-EPMC10135057 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature