Supplemental data. A simple and effective cleavable linker for chemical proteomics applications



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Supplemental data A simple and effective cleavable linker for chemical proteomics applications Yinliang Yang, annes ahne, Bernhard Kuster, and Steven. L. Verhelst * Figure S1 Figure S2 Figure S3 Table S1 Table S2 Supplementary methods: 1 General methods 2 Detailed synthetic methods and compound characterization Abbreviations: DMF, dimethyl formamide; EtAc, ethyl acetate; PE, petroleum ether 40-60; TIS, triisopropyl silane. 1

Figure S1. Cleavage of diol-dcg-04. A. diol-dcg-04 was treated with 10 mm ai 4 and analyzed by LC-MS. B. diol-dcg-04 (10 M) was treated with 10 mm ai 4 in the presence of bradykinin (10 M), purified on a vivapure C18 spin column, and analyzed by LC-MS. 2

Figure S2. Diol-DCG-04 and DCG-04 labeled cathepsins in rat liver lysate. Rat liver lysate (1 mg/ml total protein, p 5.5 in 50 mm acetate buffer, 2 mm DTT, 5 mm MgCl 2 ) were treated with diol-dcg-04 and DCG-04 (1µM, 0.5h). Labeled cathepsins in rat liver lysate and the proteins were visualized by streptavidin Western blot. The diol-dcg-04 labeled cathepsins bands are competed by pretreatment with the cysteine protease inhibitor JPM-Et (50 µm, 0.5h). 3

Figure S3. ptimization of protein release. Selective (1 mm ai 4 ) release followed by nonselective (SDS sample buffer boil) release of diol-dcg-04 labeled rat liver cathepsins from streptavidin beads detected by silver staining. Both a 2 h (left panel) or overnight (right panel) incubation did not result in satisfactory cleavage, as most proteins are released by the subsequent SDS treatment (right lanes). A 10 mm periodate cleavage turned out to be efficient (see Fig. 3B). 4

Table S1. The number of total and oxidized methionine residues in all identified peptides of the cathepsin targets in rat liver proteome n bead digestion Chemical cleavage Cathepsin Total Met xidized Met Total Met xidized Met Cat B 24 6 18 12 Cat Z 26 3 30 9 Cat C 3 0 3 2 Cat 6 0 6 1 Cat L 4 0 0 0 Cat J 0 0 0 0 Table S2. Spectral counts of selected cathepsin peptides in oxidized and non-oxidized form from rat liver proteome. n bead digestion Chemical cleavage Selected peptides 1 on-oxidized xidized on-oxidized xidized Cat B EAGDVMGGAIR 3 2 1 3 SGVYKEAGDVMGGAIR 3 1 2 2 Cat Z MMAEIYAGPISCGIMATER 2 1 1 4 Cat C QESCGSCYSFASLGMLEAR 2 0 1 1 Cat GIMGEDSYPYIGK 2 0 2 1 1 xidized methionines are indicated in bold 5

Supplemental methods 1 General methods Unless otherwise noted, all reagents were purchased from commercial suppliers and used without further purification. Reactions were analyzed by thin-layer chromatography on 0.20 mm silica plates with fluorescent indicator. All LC-MS analysis was done with an agilent 6210 LCMS-Systhem using a custom-made C18 column. Flash chromatography was carried out with 230-400 mesh silica gel. Reverse-phase PLC was conducted on Waters 515 PLC System using a Waters x-bridge reversed-phase C18 column. Purifications were performed at room temperature and compounds were eluted with increasing concentration of acetonitrile (solvent A: 0.1% TFA in water, solvent B: 0.1% TFA in acetonitrile). 2 Synthesis Synthesis of cleavable building block The synthesis of the cleavable building block 1 follows the procedure as outlined in Figure S4. Figure S4. Synthetic scheme for 1 Dimethyl 2,3--isopropylidene-L-tartrate (5) L tartaric acid (10.1 g) was added to a solution of methanol (4 ml) and p-toluenesulfonic acid (40 mg) and 2, 2-dimethoxypropane (19 ml). The solution was stirred with reflux at 50 o C for 2h. Another 10 ml 2,2-dimethoxypropane and dry cyclohexane (40 ml) was added. The solution was hearted to 68 o C and refluxed for 2 days and the volatile compounds (acetone, methanol) with cyclohexane were slowly removed by simple distillation. Anhydrous potassium carbonate (100 6

mg) was added to neutralize the reaction. The solvent and unreacted 2,2-dimethoxypropane were removed under reduce pressure. The crude compound was purified by vacuum distillation and isolated as a light yellow oil (10.9 g, 74%). 1 MR (400 Mz ): 4.81 (s, 2), 3.83 (s, 6), 1.50 (s, 6). 13 C DEPT MR (400 Mz): 76.99, 52.83, 26.30. Methyl 2,3--isopropylidene-L-tartrate (1) To a solution of dimethyl 2,3--isopropylidene-L-tartrate (2.06 g, 9.468 mmol) in C 3 (20 ml) was added a solution of K (531.24 mg, 9.468 mmol) over 1h. The reaction was stirred overnight and evaporated. The resulted residue was dissolved in Et 2 (30 ml) and washed with 10 ml saturated ac 3 solution. The aqueous portion was acidified to p 3.5 with 3 M CI and extracted with Et 2 (8 x 20 ml). The combined Et 2 extracts were dried and evaporated to give colorless oil 1.21g (63%). 1 MR (400 Mz ): 4.89 (d, 1, J = 6.0 z), 4.83 (d,1, J = 5.5 z), 3.85 (s, 3), 1.53 (s,3), 1.51 (s, 3). 13 C DEPT MR (400 Mz): 77.04, 76.46, 53.03, 26.33, 26.29. Synthesis of the biotin-diol-alkyne The synthesis of the cleavable alkyne reagent 3 is performed as outlines in Figure S5. Me Me 1 propargyl amine BTU/DIEA 72% 1,8-amino-2,6-dioxaoctane, 85% S 2 6 7 3 Biotin, BTU, DIEA then, Ac/ 2 25% Figure S5. Synthesis of reagent 3. 7

Synthesis of 6 To a solution of methyl 2,3--isopropylidene-L-tartrate (1, 448 mg, 2.2 mmol) in DMF (10 ml) was added propargylamine-hydrochlorid (183 mg, 2 mmol), BTU (758 mg, 2 mmol) and DIEA (690 µl, 4 mmol), The reaction was stirred overnight and evaporated. The resulted residue was dissolved in DCM and washed with saturated ac 3, 1 M KS 4 and brine. The organic layer was dried on MgS 4 and concentrated under reduced pressure. Silica column chromatograph (10 40% EtAc in PE) afforded the title compound (347.4 mg, 72%). ESI-MS: [M+] + calculated for C 11 15 5 242.0950, found 242.1047. 1 MR (400 Mz ): 6.7 (bs, 1), 4.79 (d, 1, J = 5.0 z), 4.76 (d, 1, J = 5.0 z), 4.17-4.04 (m, 2), 3.83 (s, 3), 2.27 (t, 1, J = 2.4 z), 1.51 (s, 3), 1.49 (s, 3). 13 C DEPT MR (400 Mz): 77.68, 77.30, 52.89, 38.62, 28.88, 26.60, 26.22. Synthesis of 7 To a solution of 6 (183 mg, 0.76 mmol) in toluene (1 ml) was added 1,8-diamino-3,6- dioxaoctane (555 µl, 3.8 mmol). The reaction was stirred at 80 o C overnight. The solvents were evaporated in vacuo, and the product was purified to homogeneity by silica gel chromatography (Me/DCM/ 4 0/10/0.1 to 1/10/0.1) to yield compound 7 (231mg, 0.646 mmol, 85%). ESI-MS: [M+] + calculated for C 16 27 3 6 358.1900, found 358.2207. 1 MR (400 Mz ): 7.40 (bs, 1), 7.22 (bs, 1), 4.61 (d, 1, J = 6.8 z), 4.58 (d, 1, J = 7.2 z), 4.17-4.05 (m, 2), 3.65-3.46 (m, 10), 2.88 (t, 2h, J = 5.2 z), 2.25 (t, 2, J = 2.4 z), 1.54 (bs, 2), 1.51 (s, 3), 1.49 (s, 3). 13 C DEPT MR (400 Mz): 77.46, 77.29, 73.48, 70.46, 70.26, 69.55, 41.75, 39.04, 28.98, 26.22, 26.07. Synthesis of cleavable alkyne-biotin reagent 3 To a solution of 7 in DMF (728 µl) was added biotin (39.2 mg), BTU (60.9 mg) and DIEA (27.6 µl), and the reaction was stirred overnight. The solvents were evaporated in vacuo, 90% Ac in water (3 ml) was added, and the mixture was stirred at 80 o C overnight. Solvents were evaporated in vacuo and the product was purified by PLC to yield 20 mg (25%) of the title compound. ESI-MS: [M+] + calculated for C 26 41 5 8 S 544.2363, found 544..2407; 1 MR (400 Mz ): 8.06 (t, 1, J = 5.6 z), 7.83 (t, 1, J = 5.6 z), 7.63 (t, 1, J = 6.0 z), 6.41 (bs, 2), 4.30 (dd, 1, J = 7.6 z, J = 5.2 z), 4.24 (dd, 2, J = 8.8 z, J = 1.6 z), 4.13 (dd, 1, J 8

= 7.6 z, J = 4.4 z), 3.96-3.56 (m, 2 + DMS), 3.51 (m, 4), 3.44(t, 2, J = 6.0 z), 3.40 (t, 2, J = 6.0 z), 3.1-3.1 (m, 5), 3.05 (d, 1, J = 2.4 z), 2.82 (dd, 1, J = 5.2 z, J = 12.4 z), 2.58 (d, 1, J = 12.4 z), 2.07 (t, 2, J = 7.2 z), 1.65-1.25 (m, 6). Synthesis of diol-dcg-04 Solid phase peptide synthesis was performed on Rink resin as shown in Figure S6, using Fmocamino acid/dic/bt (3eq/3eq/3eq with respect to the loading reported by the supplier; final concentration ~ 0.3 M) in DMF for 3-5h at room temperature. After the coupling of methyl 2,3- -isopropylidene-l-tartrate under the same conditions as for amino acids, 8-diamino-3,6- dioxaoctane (1 ml) was added and the resin was shaken overnight. ext, the tyrosine and leucine building blocks were introduced and finally, the epoxysuccinate warhead (1.5 eq) was coupled with DIC/Bt overnight. The probes were cleaved by incubation with a solution of TFA: TIS: 2 (90%: 2.5%: 7.5%) for 3 hours. The peptide was precipitated in cold diethyl ether and purified by PLC yielding a white solid (17%). ESI-MS: [M+] + calculated for C 47 73 9 16 S 1052.4896, found 1052.4897. 1 MR (400 Mz ): 8.52 (d, 1, J = 4.4 z), 8.08 (d, 1, J = 8.0 z), 7.9 (t, 1, J = 5.6 z), 7.73 (t, 1, J = 5.6 z), 7.68 (d, 1h, J = 8.0 z), 7.65 (t, 1, J = 6.0 z), 7.35 (s, 1), 7.16 (s, 1), 6.97 (d, 2, J = 8.4 z), 6.61 (d, 2, J = 8.4 z), 6.42 (bs, 2), 4.39-4.27 (m, 4), 4.24-4.11 (m, 5), 3.71 (d, 1, J = 1.6 z), 3.59 (d, 1, J = 2.0 z), 3.54-3.46 (m, 4), 3.43 (t, 2, J = 6.0 z), 3.38-3.07 (m, 7), 3.01-2.94 (m, 2), 2.82(dd, 2, J = 5.2 z, J = 12.8 z), 2.71-2.65 (m, 1), 2.57(d,1, J = 12.4 z), 2.035 (t, 2, J = 7.2 z), 1.75-1.28 (m, 15), 1.23 (t, 3, J = 7.2 z), 0.86 (d, 3, J = 6.4 z), 0.822 (d, 3, J = 6.4 z). 9

Fmoc a, b, c 2 Rink Resin S d, e, f 2 Et S 2 diol-dcg-04 Figure S6. Synthesis of diol-dcg-04. a) 20% piperidine in DMF, then Fmoc-Lys(biotin)-, DIC, Bt; b) 20% piperidine in DMF, then building block 1, DIC, Bt; c) 1, 8-diamino-3,6- dioxaoctane, overnight; d) Fmoc-Tyr-, DIC, Bt; e) 20% piperidine in DMF, Fmoc-Leu-, DIC, Bt; f) 20% piperidine in DMF, ethyl (2S, 3S) epoxysuccinate, DIC, Bt; then TFA: TIS: 2 (90%: 2.5%: 7.5%) for 3 hours, 17% after PLC purification. 10