Table 2 Peptide profiling of 120 min duodenal digests of wheat LTP alone and in the presence of 0.26 mM linoleic acid determined by MALDI-ToF mass spectrometry.

From: Ligand binding to an Allergenic Lipid Transfer Protein Enhances Conformational Flexibility resulting in an Increase in Susceptibility to Gastroduodenal Proteolysis

LTP fragments

m/z

Normalised relative intensity

Observed

Calculated

Wheat LTP alone

Wheat LTP + linoleic acid

Intact protein (residues 1–90)

10063.22

10063.18

518

705

1–34

3474.74

3474.93

160

292

1–39

4310.6

4309.77

2546

3290

1–56

6243.58

6242.91

537

1047

1–67

7477.3

7477.18

214

290

1–79

8803.44

8803.75

270

2300

17–39*

2436.75

2436.65

805

1290

17–56

4370.01

4369.78

533

ND

17–61

4904.39

4904.39

90

90

40–56

1951.23

1951.15

292

ND

40–67

3185.43

3185.43

248

340

40–79

4512.11

4512.0

128

656

57–67*

1252.34

1252.29

450

ND

57–89

3739.16

3739.16

110

130

68–79*

1344.71

1344.58

334

ND

80–90*

1277.74

1277.45

1550

1200

Unassigned

3514.0

β€”

2833

1668

Unassigned

1098.54

β€”

1320

ND

Unassigned

2679.24

β€”

1373

1927

Unassigned

4334.4

β€”

1027

1070

Unassigned

5032.13

β€”

435

ND

Unassigned

5379.31

β€”

479

ND

Unassigned

5794.72

β€”

1004

ND

Unassigned

8673.0

β€”

312

400

  1. Peptide assignments were derived from comparison of experimentally derived masses with those obtained through in silico digestion of wheat LTP (Uniprot ID P24296, Figure S2) with trypsin and chymotrypsin. Peptide assignments corresponding to the most intense mass events are in bold. Asterisks denote peptides that were confirmed by LC-MS/MS. ND- not detected.