Enhancement of Structural Stability and IgG Affinity of a <i>Z34C</i>-Derived α-Helical Peptide via Lactam Stapling.

ABSTRACT:

Background

The Fc region of immunoglobulin G (IgG) is a key target in therapeutic and analytical applications, such as antibody purification and site-specific bioconjugation. Although Protein A exhibits strong Fc-binding affinity, its large molecular weight and limited chemical flexibility pose challenges for use in compact or chemically defined systems. To address these limitations, we designed two α-helical peptides, SpA h1 and SpA h2, based on the Fc-binding helices of the Z34C domain from Staphylococcus aureus Protein A.

Method

To enhance the structural stability and Fc-binding capability of these peptides, a lactam-based stapling strategy was employed by introducing lysine and glutamic acid residues at positions i and i + 4.

Result

The result

SUBMITTER: Lee JG 

PROVIDER: S-EPMC12729524 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature