Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility

Aurelio Mollo; Emma Y Cool; Bahar Sakar; Kushol Gupta; Elizabeth Nolan

doi:10.1039/d6sc02543a

January 1, 2026Chemical ScienceOpen Access

Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility

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Key Points

This research aims to investigate how the formation of an intradimer disulfide bond in calprotectin influences its metal-withholding ability and susceptibility to proteolysis.
Characterized calprotectin's structure to analyze disulfide bond formation.
Examined the functional role of the disulfide bond in metal sequestration and proteolysis.
Used comparison of wild-type and mutant forms of calprotectin.
Formation of the intradimer disulfide bond significantly enhances metal-binding capacity.
Mutant calprotectin showed increased susceptibility to proteolysis compared to the wild type.
Metal-sequestration function was confirmed to be linked to the structural integrity provided by the disulfide bond.

Implication

Examines how disulfide bond impacts metal withholding in calprotectin, suggesting significant roles in immunity.

Abstract

Human calprotectin (CP, S100A8/S100A9 oligomer, MRP8/MRP14 oligomer) is a metal-sequestering protein that contributes to nutritional immunity. Each human CP subunit contains a single Cys residue—Cys42 in S100A8 and Cys3 in...

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Cite This Study

Mollo et al. (2026) studied this question.

synapsesocial.com/papers/6a23bb7971a5da9775e7700e https://doi.org/10.1039/d6sc02543a

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Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility

Key Points

Implication

Abstract

Discussion

Cite This Study

Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility

Key Points

Implication

Abstract

Discussion

Cite This Study

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