An Analytical Method for Assessing Optimal Storage Conditions of Gingival Crevicular Fluid and Disclosing a Peptide Biomarker Signature of Gingivitis by MALDI‐TOF MS

Abstract

The method described provides a rapid comparative analysis of GCF signatures between periodontally healthy and gingivitis subjects. A pattern based on the expression of endogenous peptides and their PTMs is identified in GCF as putative biomarkers of gingivitis. These findings improve the knowledge of the inflammatory, immune, and structural substrates which might have a key role in the pathogenesis of gingivitis.

Gingival Crevicular Fluid Peptidome Profiling in Healthy and in Periodontal Diseases

“…Generally, the peptide profiling investigations that we summarize in this review make use of surface enhanced laser desorption ionization (SELDI) [17,18] and matrix-assisted laser desorption ionization (MALDI)-MS [6,[19][20][21][22][23][24][25][26] approaches which result more suitable and easily applicable for the analysis of natural peptides of GCF (Table 1). However, few investigations based on electrospray ionization (ESI)-MS have also been carried out to explore peptidic components and small proteins found in GCF in a top-down fashion [27][28][29] (Table 1).…”

“…Peptidomics workflow, without a digestion step, allows to preserve the endogenous information of peptides from GCF, including post-translational modifications and proteolytic products. (21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35) and (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35), Fibrinopeptide B Generally, the peptide profiling investigations that we summarize in this review make use of surface enhanced laser desorption ionization (SELDI) [17,18] and matrix-assisted laser desorption ionization (MALDI)-MS [6,[19][20][21][22][23][24][25][26] approaches which result more suitable and easily applicable for the analysis of natural peptides of GCF (Table 1). However, few investigations based on electrospray ionization (ESI)-MS have also been carried out to explore peptidic components and small proteins found in GCF in a top-down fashion [27][28][29]…”

“…Some, but not many investigations based on MS have been performed to explore the GCF peptidome both under physiological [20,22,23,27,28] and pathological conditions [6,[16][17][18][19]21,[24][25][26]29]. Targeted identifications of specific peptidic component in GCF have been reported by Lundy et al [16].…”

“…All these features make MALDI-TOF MS highly suitable for diagnostic purposes [59][60][61][62][63]. The versatility of the MALDI-TOF MS platform was exploited in different approaches to analyze GCF peptidome [6,[19][20][21][22][23][24][25][26].…”

“…However, an important limitation, as pointed out by the authors themselves, is the absence of any kind of normalization for protein concentration. Furthermore, samples stored for the same amount of time need to be compared in order to ensure the robustness of the results; indeed, as discussed above, the protein profile of a sample analyzed immediately by MS may not be comparable to that of the same sample stored at −20 • C and analyzed within 24 h [23,24].…”