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Figure S1. X-ray powder diffraction pattern a) and Nitrogen adsorption-desorption isotherm b) of synthesized MPAS. A type IV reversible isotherm is obtained with a sharp capillary condensation step that corresponds to mesopore filling.

Figure S2. Barret–Joyner–Halenda (BJH) adsorption pore size distribution of synthesized MPAS. The BJH adsorption average pore size distribution is centered at 3 nm and it is representative of micelles-templated mesopores with homogeneous diameter.

Figure S3. Saturation curves of MPAS for plasma and SF. Increasing volumes of plasma and SF (reported on the x axes) were loaded on MPAS and total protein content of eluate solution was assayed by BCA (reported on the ordinates axes). The data are the average of three independent experiments and SD are reported.

Figure S4. MALDI-TOF mass spectra of a) unprocessed synovial fluid (control) in m/z range from 950 to 6000, b) synovial fluid processed by using MPAS in m/z range from 950 to 6000. In c) and d) an in depth zooming of the m/z ranges from 910 to 1500 and from 1500 to 2500, respectively, is given.

Figure S5. MALDI-TOF mass spectra of a) unprocessed human plasma (control) in m/z range from 1100 to 6000, b) human plasma processed by using MPAS in m/z range from 1100 to 6000. In c), d) and e) an in depth zooming of the m/z ranges from 1100 to 1700, 1700 to 2400 and 2500 to 3300, respectively, is given.

Figure S6. Comparison of the positive ion MALDI mass spectra in DHB of human synovial fluid extracted by MPAS (a) and MPS (b). The asterisks indicate peaks arising from DHB matrix. Main phospholipid species selectively extracted by MPAS (a) are grouped with parenthesis and indicated with their abbreviation. LPC lyso-phosphatidylcholine, SM sphingomyelin, PC phosphatidylcholine.

Figure S7. Negative ion MALDI-TOF mass spectrum in 9-AA of synovial fluid extracted from MPAS. PC, PE and PS stand for phosphatidylcholine, phosphatidylethanolamine and phosphatidylserine, respectively. The peaks which can be assigned as PC or PE are indicated in the spectrum. Possible PS species are also evidenced.

Figure S8. Assessment of repeatibility of MALDI-TOF synovial fluid peptidic profiles by using three different batches of MPAS. Each column (a), (b) and (c) reports the MALDI traces from each batch preparation. The same SF sample was divided into nine aliquots (three for each batch), which were independently processed by MPAS procedure. The MALDI mass spectra were measured in linear mode using CHCA as matrix. To better highlight the pattern reproducibility, relative intensity is displayed in the range from 0 to 10%. The traces are shown in the m/z range from 800 to 4000.

Figure S9. Assessment of repeatibility of MALDI-TOF synovial fluid lipid profiles by using three different batches of MPAS. Each column (a), (b) and (c) reports the MALDI traces from each batch preparation. The same SF sample was divided into nine aliquots (three for each batch), which were independently processed by MPAS procedure. The positive MALDI mass spectra were measured in reflector ion mode using DHB as matrix. To better highlight the pattern reproducibility, relative intensity is displayed in the range from 0 to 60%. m/z range is reported in the range from 700 to 850.

Table S1. MS/MS sequences of some selected endogenous peptide fragment detected in the MALDI-TOF/TOF spectra of both synovial fluid and plasma. The identity of the protein precursor from which the peptide fragments originate is reported.

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