Effects of Dimerization, Dendrimerization, and Chirality in p-BthTX-I Peptide Analogs on the Antibacterial Activity and Enzymatic Inhibition of the SARS-CoV-2 PL^pro Protein.

ABSTRACT: Recent studies have shown that the peptide [des-Cys¹¹,Lys¹²,Lys¹³-(p-BthTX-I)₂K] (p-Bth) is a p-BthTX-I analog that shows enhanced antimicrobial activity, stability and hemolytic activity, and is easy to obtain compared to the wild-type sequence. This molecule also inhibits SARS-CoV-2 viral infection in Vero cells, acting on SARS-CoV-2 PL^pro enzymatic activity. Thus, the present study aimed to assess the effects of structural modifications to p-Bth, such as dimerization, dendrimerization and chirality, on the antibacterial activity and inhibitory properties of PL^pro. The results showed that the dimerization or dendrimerization of p-Bth was essential for antibacterial activity, as the monomeric structure led to a total loss o

SUBMITTER: Bitencourt NV 

PROVIDER: S-EPMC9964244 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature