PEGylation of the antimicrobial peptide LyeTx I-b maintains structure-related biological properties and improves selectivity.

ABSTRACT: The biological activity of antimicrobial peptides and proteins is closely related to their structural aspects and is sensitive to certain post-translational modifications such as glycosylation, lipidation and PEGylation. However, PEGylation of protein and peptide drugs has expanded in recent years due to the reduction of their toxicity. Due to their size, the PEGylation process can either preserve or compromise the overall structure of these biopolymers and their biological properties. The antimicrobial peptide LyeTx I-b_cys was synthesized by Fmoc strategy and coupled to polyethylene glycol 2.0 kDa. The conjugates were purified by HPLC and characterized by MALDI-ToF-MS analysis. Microbiological assays with LyeTx I-b_cys and LyeTx I-bPEG were performed against Staphy

SUBMITTER: Moreira Brito JC 

PROVIDER: S-EPMC9611540 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature