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Updated: May 18, 2026

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
Published on: January 12, 2024
Identification and characterization of histatin 1 salivary complexes by using mass spectrometry
Walter L Siqueira1, Young Ho Lee, Yizhi Xiao
1Department of Biochemistry, School of Dentistry, Schulich School of Medicine & Dentistry, Western University, London, ON, Canada. walter.siqueira@schulich.uwo.ca
Abstract:
With recent progress in the analysis of the salivary proteome, the number of salivary proteins identified has increased dramatically. However, the physiological functions of many of the newly discovered proteins remain unclear. Closely related to the study of a protein's function is the identification of its interaction partners. We investigated interactions among and functions of histatin 1 and the other proteins that are present in saliva by using high-throughput mass spectrometric techniques. This led to the identification of 43 proteins able to interact with histatin 1. In addition, we found that these protein-protein interactions protect complex partners from proteolysis and modulate their antifungal activity. Our data contribute significantly to characterization of the salivary interactome and to understanding the biology of salivary protein complexes.
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