[ CAS No. 136083-57-3 ] {[proInfo.proName]}

Name: 136083-57-3|Fmoc-D-Asp-OH|97%
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SKU: A340299
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Quality Control of [ 136083-57-3 ]

COA NMR CNMR HPLC LC-MS

Related Doc. of [ 136083-57-3 ]

SDS Specification

Alternatived Products of [ 136083-57-3 ]

Product Details of [ 136083-57-3 ]

CAS No. :	136083-57-3	MDL No. :	MFCD01318740
Formula :	C₁₉H₁₇NO₆	Boiling Point :	-
Linear Structure Formula :	-	InChI Key :	KSDTXRUIZMTBNV-MRXNPFEDSA-N
M.W :	355.34	Pubchem ID :	7006674
Synonyms :

Calculated chemistry of [ 136083-57-3 ]

Physicochemical Properties

Num. heavy atoms :	26
Num. arom. heavy atoms :	12
Fraction Csp3 :	0.21
Num. rotatable bonds :	8
Num. H-bond acceptors :	6.0
Num. H-bond donors :	3.0
Molar Refractivity :	91.75
TPSA :	112.93 Å²

Pharmacokinetics

GI absorption :	High
BBB permeant :	No
P-gp substrate :	Yes
CYP1A2 inhibitor :	Yes
CYP2C19 inhibitor :	No
CYP2C9 inhibitor :	No
CYP2D6 inhibitor :	No
CYP3A4 inhibitor :	No
Log Kp (skin permeation) :	-6.91 cm/s

Lipophilicity

Log Po/w (iLOGP) :	1.59
Log Po/w (XLOGP3) :	2.19
Log Po/w (WLOGP) :	2.45
Log Po/w (MLOGP) :	1.68
Log Po/w (SILICOS-IT) :	1.88
Consensus Log Po/w :	1.96

Druglikeness

Lipinski :	0.0
Ghose :	None
Veber :	0.0
Egan :	0.0
Muegge :	0.0
Bioavailability Score :	0.56

Water Solubility

Log S (ESOL) :	-3.24
Solubility :	0.206 mg/ml ; 0.00058 mol/l
Class :	Soluble
Log S (Ali) :	-4.2
Solubility :	0.0227 mg/ml ; 0.0000638 mol/l
Class :	Moderately soluble
Log S (SILICOS-IT) :	-4.26
Solubility :	0.0196 mg/ml ; 0.0000551 mol/l
Class :	Moderately soluble

Medicinal Chemistry

PAINS :	0.0 alert
Brenk :	0.0 alert
Leadlikeness :	2.0
Synthetic accessibility :	3.8

Safety of [ 136083-57-3 ]

Signal Word:	Warning	Class:	N/A
Precautionary Statements:	P261-P305+P351+P338	UN#:	N/A
Hazard Statements:	H302-H315-H319-H335	Packing Group:	N/A
GHS Pictogram:

Application In Synthesis of [ 136083-57-3 ]

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

Upstream synthesis route of [ 136083-57-3 ]
Downstream synthetic route of [ 136083-57-3 ]

[ 136083-57-3 ] Synthesis Path-Upstream 1~9

1
[ 56-84-8 ]
[ 102774-86-7 ]
[ 136083-57-3 ]

Yield	Reaction Conditions	Operation in experiment
92%	With sodium carbonate In water; N,N-dimethyl-formamide at 0 - 20℃; for 1 h;	3.03 g (22.8 mmol; 1.2 eq.) of L-aspartic acid (Fluka) are dissolved in 54 ml (68.8 mmol; 3.6 eq.) of a 13.5percent (m/v) aqueous sodium carbonate solution, in a dry 250 ml round-bottomed flask. The medium is cooled in an ice bath at 0° C., then a solution of 6.41 g (19.0 mmol; 1 eq.) of N-(9-fluorenylmethoxycarbonyloxy)succinimide (N-Fmoc) dissolved in 44 ml of DMF is added with vigorous stirring (a precipitate forms in the reaction medium). The stirring is maintained for 1 hour at ambient temperature. The mixture is then diluted in 665 ml of water, and extracted with ether (180 ml) then with ethyl acetate (260 ml). The resulting aqueous phase is cooled in an ice bath and acidified to pH 2 with concentrated (6 N) hydrochloric acid. The aqueous phase containing the precipitated product (in the form of an oil) is extracted with ethyl acetate (660 ml). The organic phase derived from the extraction is washed with a saturated aqueous sodium chloride solution (335 ml), and then with water (2*35 ml), dried over sodium sulphate, and concentrated in a rotary evaporator (35° C.) until a small residual volume is obtained. Compound 17 is recrystallized by adding petroleum ether (approximately 10 times the residual volume) with vigorous stirring. After having allowed the mixture to separate by settling out for 2 hours at 4° C., the precipitate is filtered off and then dried for 24 hours in a vacuum oven. 6.22 g (17.5 mmol) of compound 17 are isolated in the form of a fine white powder. Empirical formula: C₁₉H₁₇NO₆, M=355.35 g.mol^-1 Yield: 92percent M.p.: 181° C. TLC: R_f=0.8 eluent: 60percent AcOH/BuOH 4/6 (v/v) ESI-MS +: m/z measured at 378.1 [M+Na]⁺, calculated at 378.1 for C₁₉H₁₇NO₆Na ¹H NMR (dmso-d₆, 500.13 MHz) δ (ppm): 12.60 (broad s, 2H, COOH); 7.89 (d, 2H, H-4/H-4', ³J_4-3=³J_4'-3'=7.5 Hz); 7.72 (d, 1H, N_αH); 7.70 (d, 2H, H-1/H-1', ³J_1-2=³J_1'-2'=7.5 Hz); 7.42 (t, 2H, H-3/H-3', ³J_3-2=³J_3-4=³J_3'-2'=³J_3'-4'=7.5 Hz); 7.33 (t, 2H, H-2/H-2', ³J_2-1=³J_2-3=³J_2'-1'=³J_2'-3'=7.5 Hz); 4.34 (m, 1H, H-α); 4.29 (d, 2H, H-8); 4.22 (t, 1H, H-7); 2.73 (dd, 1H, H-β,³J_β-α=5.5 Hz, ³J_β-β'=16.4 Hz); 2.58 (dd, 1H, H-β', ³J_β'-α=8.3 Hz, ³J=16.4 Hz) ¹³C NMR (dmso-d₆, 125.77 MHz) δ (ppm): 172.8, 171.8 (C_αH-COOH, C_βH₂-COOH); 155.9 (C-9); 143.9 (C-5/C-5'); 140.8 (C-6/C-6'); 127.7 (C-3/C-3'); 127.2 (C-2/C-2'); 125.4 (C-1/C-1'); 120.2 (C-4/C-4'); 65.8 (C-8); 50.6 (C-α); 46.7 (C-7); 36.1 (C-β)

Reference： [1] Patent: US2007/142324, 2007, A1, . Location in patent: Page/Page column 8

2
[ 129460-09-9 ]
[ 136083-57-3 ]

Reference： [1] Tetrahedron Letters, 1992, vol. 33, # 37, p. 5441 - 5444
[2] Journal of Organic Chemistry, 2006, vol. 71, # 24, p. 9045 - 9050

3
[ 71989-14-5 ]
[ 136083-57-3 ]

Reference： [1] Chemistry - A European Journal, 2015, vol. 21, # 31, p. 11014 - 11016
[2] Journal of Peptide Science, 2010, vol. 16, # 3, p. 159 - 164
[3] Organic Letters, 2012, vol. 14, # 24, p. 6346 - 6349

4
[ 56-84-8 ]
[ 28920-43-6 ]
[ 136083-57-3 ]

Reference： [1] Journal of Organic Chemistry, 2011, vol. 76, # 16, p. 6825 - 6831
[2] Journal of the Chinese Chemical Society, 2011, vol. 58, # 4, p. 509 - 515

5
[ 146982-24-3 ]
[ 136083-57-3 ]

Reference： [1] Chemistry - A European Journal, 2015, vol. 21, # 31, p. 11014 - 11016

6
[ 56-84-8 ]
[ 82911-69-1 ]
[ 136083-57-3 ]

Reference： [1] Chemical and Pharmaceutical Bulletin, 1988, vol. 36, # 10, p. 3915 - 3919
[2] Tetrahedron Letters, 2009, vol. 50, # 46, p. 6351 - 6354

7
[ 1415814-25-3 ]
[ 136083-57-3 ]
[ 54711-38-5 ]

Reference： [1] Journal of Photochemistry and Photobiology A: Chemistry, 2012, vol. 241, p. 52 - 57

8
[ 1415814-26-4 ]
[ 1415814-22-0 ]
[ 136083-57-3 ]

Reference： [1] Journal of Photochemistry and Photobiology A: Chemistry, 2012, vol. 241, p. 52 - 57

9
[ 136083-57-3 ]
[ 107-18-6 ]
[ 144120-53-6 ]

Reference： [1] Synthesis, 2009, # 5, p. 809 - 814

[ 136083-57-3 ] Synthesis Path-Downstream 1~88

1
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 73724-45-5 ]
Fmoc-Val, Fmoc-Fen, Ac₂O [ No CAS ]
(S)-3-{(S)-2-[(R)-2-({(S)-1-[(S)-2-((S)-2-Acetylamino-3-[1,10]phenanthrolin-2-yl-propionylamino)-3-methyl-butyryl]-pyrrolidine-2-carbonyl}-amino)-3-hydroxy-propionylamino]-3-phenyl-propionylamino}-succinamic acid [ No CAS ]

Reference： [1]Journal of the American Chemical Society,1996,vol. 118,p. 11349 - 11356

2
[ 68858-20-8 ]
[ 112883-29-1 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
N^α-Fmoc-O-(2,3,4,6-tetra-O-benzoyl-β-D-glucopyranosyl)-Ser-OPfp [ No CAS ]
C₇₇H₇₇N₉O₁₉ [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry Letters,1996,vol. 6,p. 367 - 372

3
[ 68858-20-8 ]
[ 136083-57-3 ]
[ 105047-45-8 ]
[ 35737-15-6 ]
N^α-Fmoc-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)Tyr-OPfp [ No CAS ]
C₇₁H₈₆N₁₂O₁₉ [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry Letters,1996,vol. 6,p. 367 - 372

4
[ 68858-20-8 ]
[ 112883-29-1 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
Fmoc-Lys-OH, N^α-Fmoc-N^γ-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-Asn-OPfp [ No CAS ]
C₇₅H₉₂N₁₄O₂₁ [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry Letters,1996,vol. 6,p. 367 - 372

5
[ 68858-20-8 ]
[ 112883-29-1 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
Fmoc-Lys-OH, N^α-Fmoc-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)Tyr-OPfp [ No CAS ]
C₈₀H₉₅N₁₃O₂₁ [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry Letters,1996,vol. 6,p. 367 - 372

6
[ 68858-20-8 ]
[ 112883-29-1 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
Fmoc-Lys-OH, N^α-Fmoc-O-(2,3,4,6-tetra-O-benzoyl-β-D-glucopyranosyl)-Ser-OPfp [ No CAS ]
C₉₄H₉₉N₁₃O₂₁ [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry Letters,1996,vol. 6,p. 367 - 372

7
[ 68858-20-8 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
N^α-Fmoc-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)Tyr-OPfp [ No CAS ]
C₅₄H₆₄N₈O₁₇ [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry Letters,1996,vol. 6,p. 367 - 372

8
[ 29022-11-5 ]
[ 136083-57-3 ]
[ 91000-69-0 ]
[ 132684-59-4 ]
R-Fmoc-Ahd [ No CAS ]
[(2S,8S,11S,14S)-8-(3-Guanidino-propyl)-3,6,9,12,15-pentaoxo-14-phenethyl-11-tetradecyl-1,4,7,10,13-pentaaza-cyclopentadec-2-yl]-acetic acid [ No CAS ]

Reference： [1]Helvetica Chimica Acta,1997,vol. 80,p. 1280 - 1300

9
[ 29022-11-5 ]
[ 136083-57-3 ]
[ 91000-69-0 ]
[ 132684-59-4 ]
Fmoc-Ahd [ No CAS ]
[(2S,8S,11R,14S)-8-(3-Guanidino-propyl)-3,6,9,12,15-pentaoxo-14-phenethyl-11-tetradecyl-1,4,7,10,13-pentaaza-cyclopentadec-2-yl]-acetic acid [ No CAS ]

Reference： [1]Helvetica Chimica Acta,1997,vol. 80,p. 1280 - 1300

10
[ 29022-11-5 ]
[ 136083-57-3 ]
[ 132684-59-4 ]
[ 193885-60-8 ]
Fmoc Arg [ No CAS ]
[(2S,8S,11S,14R)-8-(3-Guanidino-propyl)-3,6,9,12,15-pentaoxo-14-phenethyl-11-tetradecyl-1,4,7,10,13-pentaaza-cyclopentadec-2-yl]-acetic acid [ No CAS ]

Reference： [1]Helvetica Chimica Acta,1997,vol. 80,p. 1280 - 1300

11
[ 29022-11-5 ]
[ 136083-57-3 ]
[ 91000-69-0 ]
[ 132684-59-4 ]
Fmoc-HdGly [ No CAS ]
[(2S,8S,14S)-8-(3-Guanidino-propyl)-10-hexadecyl-3,6,9,12,15-pentaoxo-14-phenethyl-1,4,7,10,13-pentaaza-cyclopentadec-2-yl]-acetic acid [ No CAS ]

Reference： [1]Helvetica Chimica Acta,1997,vol. 80,p. 1280 - 1300

12
[ 136083-57-3 ]
[ 135112-28-6 ]
PG-(S)-Cys(Me)-al; MeCOX [ No CAS ]
(S)-3-Acetylamino-N-[(S)-1-((R)-1-formyl-2-methylsulfanyl-ethylcarbamoyl)-butyl]-succinamic acid [ No CAS ]

Reference： [1]Organic Letters,2000,vol. 2,p. 19 - 22

13
[ 136083-57-3 ]
[ 95107-99-6 ]
[ 135112-28-6 ]
MeCOX [ No CAS ]
(S)-3-Acetylamino-N-[(S)-1-((S)-1-formyl-but-3-enylcarbamoyl)-butyl]-succinamic acid [ No CAS ]

Reference： [1]Organic Letters,2000,vol. 2,p. 19 - 22

14
[ 136083-57-3 ]
[ 135112-28-6 ]
PG-(S)-propargyl Gly-al; MeCOX [ No CAS ]
(S)-3-Acetylamino-N-[(S)-1-((S)-1-formyl-but-3-ynylcarbamoyl)-butyl]-succinamic acid [ No CAS ]

Reference： [1]Organic Letters,2000,vol. 2,p. 19 - 22

15
[ 136083-57-3 ]
[ 135112-28-6 ]
PG-(S)-Cys(Me)-al; PhCOX [ No CAS ]
(S)-3-Benzoylamino-N-[(S)-1-((R)-1-formyl-2-methylsulfanyl-ethylcarbamoyl)-butyl]-succinamic acid [ No CAS ]

Reference： [1]Organic Letters,2000,vol. 2,p. 19 - 22

16
[ 136083-57-3 ]
[ 95107-99-6 ]
[ 135112-28-6 ]
PhCOX [ No CAS ]
(S)-3-Benzoylamino-N-[(S)-1-((S)-1-formyl-but-3-enylcarbamoyl)-butyl]-succinamic acid [ No CAS ]

Reference： [1]Organic Letters,2000,vol. 2,p. 19 - 22

17
[ 136083-57-3 ]
[ 135112-28-6 ]
PG-(S)-propargyl Gly-al; PhCOX [ No CAS ]
(S)-3-Benzoylamino-N-[(S)-1-((S)-1-formyl-but-3-ynylcarbamoyl)-butyl]-succinamic acid [ No CAS ]

Reference： [1]Organic Letters,2000,vol. 2,p. 19 - 22

18
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 136083-57-3 ]
[ 108-24-7 ]
[ 77128-73-5 ]
3-[2-(2-acetylamino-acetylamino)-4-methyl-pentanoylamino]-N-(1-carbamoyl-2-phenyl-ethyl)-N-methyl-succinamic acid [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2000,vol. 43,p. 103 - 113

19
[ 29022-11-5 ]
[ 136083-57-3 ]
[ 108-24-7 ]
[ 105047-45-8 ]
[ 77128-73-5 ]
(S)-3-((S)-2-{(S)-2-[(2-Acetylamino-acetyl)-methyl-amino]-3-phenyl-propionylamino}-6-amino-hexanoylamino)-succinamic acid [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2000,vol. 43,p. 103 - 113

20
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 67436-13-9 ]
Fmoc-Arg(Pmc)-OHFmoc-His(Trt)-OH [ No CAS ]
S-tert-butyl-Cys⁽⁵⁾-angiotensin II [ No CAS ]

Reference： [1]Arzneimittel-Forschung/Drug Research,2000,vol. 50,p. 526 - 529

21
[ 29022-11-5 ]
[ 136083-57-3 ]
[ 91000-69-0 ]
[ 77128-72-4 ]
[ 76-05-1 ]
H-Arg-Gly-Asp-Tyr(Me)-NH₂*2TFA [ No CAS ]

Reference： [1]Tetrahedron Letters,2006,vol. 47,p. 8205 - 8207

22
[ 136083-57-3 ]
[ 73724-45-5 ]
[ 91000-69-0 ]
[ 135248-89-4 ]
FMOC-T [ No CAS ]
FMOC-L [ No CAS ]
cyclo(1β-7β)(CRsDTLC)-NH2 [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2002,vol. 45,p. 3451 - 3457

23
[ 136083-57-3 ]
FMOC-L [ No CAS ]
[ 162558-25-0 ]

Reference： [1]Synthetic Communications,2006,vol. 36,p. 2901 - 2912

24
[ 136083-57-3 ]
[ 104091-09-0 ]
[ 73731-37-0 ]
[ 88050-17-3 ]
[ 76-05-1 ]
C₂HF₃O₂*C₄₇H₇₂N₁₀O₁₇ [ No CAS ]

Reference： [1]Chemical Communications,2007,p. 4453 - 4455

25
[ 136083-57-3 ]
[ 107-18-6 ]
[ 144120-53-6 ]

Reference： [1]Synthesis,2009,p. 809 - 814

26
C₁₅H₁₁O₂Pol [ No CAS ]
[ 347372-11-6 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 136083-57-3 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 71989-16-7 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 144120-53-6 ]
C₈₉H₁₂₃N₁₈O₂₆Pol [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry,2010,vol. 18,p. 8388 - 8395

27
C₁₅H₁₁O₂Pol [ No CAS ]
[ 174800-19-2 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 136083-57-3 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 71989-16-7 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 144120-53-6 ]
C₉₀H₁₂₅N₁₈O₂₆Pol [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry,2010,vol. 18,p. 8388 - 8395

28
C₁₅H₁₁O₂Pol [ No CAS ]
[ 1007834-40-3 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 136083-57-3 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 71989-16-7 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 144120-53-6 ]
C₉₁H₁₂₇N₁₈O₂₆Pol [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry,2010,vol. 18,p. 8388 - 8395

29
C₁₅H₁₁O₂Pol [ No CAS ]
[ 854144-37-9 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 136083-57-3 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 71989-16-7 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 144120-53-6 ]
C₉₃H₁₃₁N₁₈O₂₆Pol [ No CAS ]

Reference： [1]Bioorganic and Medicinal Chemistry,2010,vol. 18,p. 8388 - 8395

30
[ 867062-95-1 ]
C₄₀H₃₂NO₅Pol [ No CAS ]
C₄₁H₃₀F₅₁NO₇ [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 71989-33-8 ]
[ 136083-57-3 ]
[ 71989-35-0 ]
[ 119831-72-0 ]
[ 116783-35-8 ]
[ 109425-51-6 ]
N-(12-((2-(2-((tris((4,4,5,5,6,6,7,7,8,8,9,9,10,10,11,11,11-heptadecafluoroundecyloxy)methyl)methyl)amino)-2-oxoethoxy)-1-oxoethyl)amino)-4,7,10-trioxa-dodecanoyl)-L-prolyl-L-alanyl-L-histidyl-L-glycyl-L-valyl-(O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-galactopyranosyl)-L-threonyl)-L-seryl-L-alanyl-L-prolyl-L-aspartyl-L-threonyl-L-arginyl-L-prolyl-L-alanyl-L-prolyl-L-glycyl-L-seryl-(O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-galactopyranosyl)-L-threonyl)-L-alanyl-L-proline [ No CAS ]

Reference： [1]Chemical Communications,2011,vol. 47,p. 382 - 384

31
[ 867062-95-1 ]
C₄₀H₃₂NO₅Pol [ No CAS ]
C₄₁H₃₀F₅₁NO₇ [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 71989-33-8 ]
[ 136083-57-3 ]
[ 71989-35-0 ]
[ 119831-72-0 ]
[ 116783-35-8 ]
[ 109425-51-6 ]
N-(12-((2-(2-((tris((4,4,5,5,6,6,7,7,8,8,9,9,10,10,11,11,11-heptadecafluoroundecyloxy)methyl)methyl)amino)-2-oxoethoxy)-1-oxoethyl)amino)-4,7,10-trioxa-dodecanoyl)-L-prolyl-L-alanyl-L-histidyl-L-glycyl-L-valyl-(O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-galactopyranosyl)-L-threonyl)-L-seryl-L-alanyl-L-prolyl-L-aspartyl-L-threonyl-L-arginyl-L-prolyl-L-alanyl-L-prolyl-L-glycyl-L-seryl-L-threonyl-L-alanyl-L-proline [ No CAS ]

Reference： [1]Chemical Communications,2011,vol. 47,p. 382 - 384

32
[ 867062-95-1 ]
C₄₀H₃₂NO₅Pol [ No CAS ]
C₄₁H₃₀F₅₁NO₇ [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 71989-33-8 ]
[ 136083-57-3 ]
[ 71989-35-0 ]
[ 119831-72-0 ]
[ 116783-35-8 ]
[ 109425-51-6 ]
N-(12-((2-(2-((tris((4,4,5,5,6,6,7,7,8,8,9,9,10,10,11,11,11-heptadecafluoroundecyloxy)methyl)methyl)amino)-2-oxoethoxy)-1-oxoethyl)amino)-4,7,10-trioxa-dodecanoyl)-L-prolyl-L-alanyl-L-histidyl-L-glycyl-L-valyl-L-threonyl-L-seryl-L-alanyl-L-prolyl-L-aspartyl-L-threonyl-L-arginyl-L-prolyl-L-alanyl-L-prolyl-L-glycyl-L-seryl-(O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-galactopyranosyl)-L-threonyl)-L-alanyl-L-proline [ No CAS ]

Reference： [1]Chemical Communications,2011,vol. 47,p. 382 - 384

33
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 136083-57-3 ]
[ 144120-54-7 ]
[ 1318806-36-8 ]

Reference： [1]ACS Combinatorial Science,2011,vol. 13,p. 486 - 495

34
[ 35661-39-3 ]
[ 136083-57-3 ]
[ 86123-10-6 ]
[ 144120-54-7 ]
[ 1318806-76-6 ]

Reference： [1]ACS Combinatorial Science,2011,vol. 13,p. 486 - 495

35
[ 867062-95-1 ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
N-(fluoren-9-ylmethoxycarbonyl)-C-[2,3,4-tri-O-benzyl-β-L-fucopyranosyl]-L-tyrosine [ No CAS ]
C₃₇H₃₀NO₄Pol [ No CAS ]
[ 71989-31-6 ]
[ 71989-33-8 ]
[ 136083-57-3 ]
[ 71989-35-0 ]
[ 119831-72-0 ]
[ 109425-51-6 ]
[N-(12-amino-4,7,10-trioxadodecanoyl)-L-prolyl]-L-alanyl-L-histidyl-glycyl-L-valyl-L-threonyl-L-seryl-L-alanyl-L-prolyl-L-aspartyl-L-threonyl-L-arginyl-L-prolyl-L-alanyl-L-prolyl-glycyl-(C-[2,3,4-tri-O-benzyl-β-L-fucopyranosyl]-L-tyrosyl)-L-threonyl-L-alanyl-L-prolyl-L-prolyl-L-alanine [ No CAS ]
[N-(12-amino-4,7,10-trioxadodecanoyl)-L-prolyl]-L-alanyl-L-histidyl-glycyl-L-valyl-L-threonyl-L-seryl-L-alanyl-L-prolyl-L-aspartyl-L-threonyl-L-arginyl-L-prolyl-L-alanyl-L-prolyl-glycyl-(C-[2,4-dii-O-benzyl-β-L-fucopyranosyl]-L-tyrosyl)-L-threonyl-L-alanyl-L-prolyl-L-prolyl-L-alanine [ No CAS ]

Reference： [1]Chemistry - A European Journal,2013,vol. 19,p. 7020 - 7041

36
[ 867062-95-1 ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
N-(fluoren-9-ylmethoxycarbonyl)-C-[4,6-di-O-acetyl-2,3-di-O-benzyl-β-D-glucopyranosyl]-L-tyrosine [ No CAS ]
C₃₇H₃₀NO₄Pol [ No CAS ]
[ 71989-31-6 ]
[ 71989-33-8 ]
[ 136083-57-3 ]
[ 71989-35-0 ]
[ 119831-72-0 ]
[ 109425-51-6 ]
[N-(12-amino-4,7,10-trioxadodecanoyl)-L-prolyl]-L-alanyl-L-histidyl-glycyl-L-valyl-L-threonyl-L-seryl-L-alanyl-L-prolyl-L-aspartyl-L-threonyl-L-arginyl-L-prolyl-L-alanyl-L-prolyl-glycyl-(C-[4,6-di-O-acetyl-2,3-di-O-benzyl-β-D-glucopyranosyl]-L-tyrosyl)-L-threonyl-L-alanyl-L-prolyl-L-prolyl-L-alanine [ No CAS ]

Reference： [1]Chemistry - A European Journal,2013,vol. 19,p. 7020 - 7041

37
[ 5466-06-8 ]
[ 383-70-0 ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 136083-57-3 ]
[ 91000-69-0 ]
[ 120173-57-1 ]
[ 116783-35-8 ]
[ 109425-51-6 ]
trifluoroacetyl-Gly-Val-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Thr)-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Ser)-Ala-Pro-Asp-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Thr)-Arg-Pro-Ala-Pro-Gly-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Ser)-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Thr)-Ala-Pro-Pro-Ala-His 2-(ethoxycarbonyl)ethyl thioester [ No CAS ]

Reference： [1]Biopolymers,2011,vol. 96,p. 137 - 146

38
4-sulfamylbutyryl-aminomethyl resin [ No CAS ]
[ 383-70-0 ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 136083-57-3 ]
[ 91000-69-0 ]
[ 120173-57-1 ]
[ 116783-35-8 ]
N_α-(Fluoren-9-ylmethoxycarbonyl)-N_(im)-(tert-butyloxycarbonyl)-L-histidine [ No CAS ]
trifluoroacetyl-Gly-Val-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Thr)-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Ser)-Ala-Pro-Asp-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Thr)-Arg-Pro-Ala-Pro-Gly-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Ser)-(O-(2-deoxy-2-acetylamino-3,4,6-tri-O-acetyl-α-D-galactopyranosyl)-Thr)-Ala-Pro-Pro-Ala-His 2-(ethoxycarbonyl)ethyl thioester [ No CAS ]

Reference： [1]Biopolymers,2011,vol. 96,p. 137 - 146

39
[ 7423-55-4 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 108-24-7 ]
[ 35737-15-6 ]
[ 71989-16-7 ]
[ 73724-45-5 ]
[ 159857-60-0 ]
Ac-Pro-Asn-Asn-Trp-Ala-Asp-Phe-Ser-Lys(3-maleimidopropionyl)-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2015,vol. 13,p. 8008 - 8015

40
[ 7423-55-4 ]
[ 68858-20-8 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 104091-09-0 ]
[ 108-24-7 ]
[ 71989-16-7 ]
[ 159857-60-0 ]
Ac-Phe-Glu-Asp-Asn-Phe-Val-Pro-Lys(3-maleimidopropionyl)-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2015,vol. 13,p. 8008 - 8015

41
[ 56-41-7 ]
[ 68858-20-8 ]
[ 42287-94-5 ]
[ 112883-29-1 ]
[ 71989-31-6 ]
[ 136083-57-3 ]
[ 73724-45-5 ]
C₄₇H₆₁N₉O₁₅ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: All linear peptides were assembled using standard Fmoc peptide synthesisprotocol with the Rink amide resin on 433A Peptide Synthesizer (Applied Biosystems).For each coupling reaction, 10 equiv of Fmoc-amino acid, 0.45 Msolution of HOBt/HBTU (9 equiv) in DMF, 2 M solution of DIEA in NMP wereused. The coupling reaction was allowed to proceed for 9 min. Fmoc deprotectionwas performed by treating the resin-bound peptide with 20% piperidinein DMF for 10 min. The peptide was cleaved from the resin by treating the resin with a cleavage cocktail containing 94% TFA, 2% water, 2% triisopropylsilane,2% phenol for 3 hr. All protecting groups were also removedduring this cleavage reaction. TFA was removed under reduced pressureand the peptides were precipitated in diethyl ether, centrifuged, and washedwith diethyl ether before drying in high vacuum. The crude peptides werepurified by preparative reverse phase high-performance liquid chromatography(HPLC). The final compound was characterized by NMR and MALDIMS.All compounds were > 95% purity. The synthetic approaches for123B9-L2-PTX and the scrambled XDP-L2-PTX are similar to what we haverecently reported

Reference： [1]Chemistry and Biology,2015,vol. 22,p. 876 - 887

42
[ 40047-23-2 ]
[ 56-41-7 ]
[ 68858-20-8 ]
[ 112883-29-1 ]
[ 71989-31-6 ]
[ 136083-57-3 ]
[ 73724-45-5 ]
C₄₆H₅₉N₉O₁₆ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: All linear peptides were assembled using standard Fmoc peptide synthesisprotocol with the Rink amide resin on 433A Peptide Synthesizer (Applied Biosystems).For each coupling reaction, 10 equiv of Fmoc-amino acid, 0.45 Msolution of HOBt/HBTU (9 equiv) in DMF, 2 M solution of DIEA in NMP wereused. The coupling reaction was allowed to proceed for 9 min. Fmoc deprotectionwas performed by treating the resin-bound peptide with 20percent piperidinein DMF for 10 min. The peptide was cleaved from the resin by treating the resin with a cleavage cocktail containing 94percent TFA, 2percent water, 2percent triisopropylsilane,2percent phenol for 3 hr. All protecting groups were also removedduring this cleavage reaction. TFA was removed under reduced pressureand the peptides were precipitated in diethyl ether, centrifuged, and washedwith diethyl ether before drying in high vacuum. The crude peptides werepurified by preparative reverse phase high-performance liquid chromatography(HPLC). The final compound was characterized by NMR and MALDIMS.All compounds were > 95percent purity. The synthetic approaches for123B9-L2-PTX and the scrambled XDP-L2-PTX are similar to what we haverecently reported

Reference： [1]Chemistry and Biology,2015,vol. 22,p. 876 - 887

43
[ 146982-24-3 ]
[ 136083-57-3 ]

Reference： [1]Chemistry - A European Journal,2015,vol. 21,p. 11014 - 11016

44
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 104091-09-0 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 73731-37-0 ]
[ 71989-16-7 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 91000-69-0 ]
[ 96402-49-2 ]
[ 94744-50-0 ]
Y-(α-aminoisobutyroyl)-EGTFTSDYSIYLDKKAQRAFVNWLLA-(α-aminoisobutyroyl)-KYG-(β-(1-naphthyl)-alaninoyl)-LDF-NH2 [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		Solid phase peptide synthesis was performed on a CEM Liberty Peptide Synthesizer using standard Fmoc chemistry. TentaGel S Ram resin (1 g; 0.25 mmol/g) was swelled in NMP (10 ml) prior to use and transferred between tube and reaction vessel using DCM and NMP. Coupling (0148) An Fmoc-amino acid in NMP/DMF/DCM (1:1:1; 0.2 M; 5 ml) was added to the resin in a CEM Discover microwave unit together with HATU/DMF or COMU/DMF (0.5 M; 2 ml) and DIPEA/NMP (2.0 M; 1 ml). The coupling mixture was heated to 75° C. for 5 min while nitrogen was bubbled through the mixture. The resin was then washed with NMP (4×10 ml). Deprotection (0149) Piperidine/DMF (20percent; 10 ml) was added to the resin for initial deprotection and the mixture was heated by microwaves (30 sec; 40° C.). The reaction vessel was drained and a second portion of piperidine/NMP (20percent; 10 ml) was added and heated (75° C.; 3 min.) again. The resin was then washed with DMF (6×10 ml). Side Chain Acylation (0150) Fmoc-Lys(ivDde)-OH or alternatively another amino acid with an orthogonal side chain protective group was introduced at the position of the acylation. The N-terminal of the peptide backbone was then Boc-protected using Boc2O or alternatively by using a Boc-protected amino acid in the last coupling. While the peptide was still attached to the resin, the orthogonal side chain protective group was selectively cleaved using freshly prepared hydrazine hydrate (2-4percent) in NMP for 2×15 min. The unprotected lysine side chain was first coupled with Fmoc-Glu-OtBu or another spacer amino acid, which was deprotected with piperidine and acylated with a lipophilic moiety using the peptide coupling methodology as described above. Alternatively, the acylation moiety was introduced as a premade building block e.g. Fmoc-Lys(hexadecanoyl-gamma-Glu)-OH where gamm-Glu is the coupling of Glutamic acid through the side-chain. Abbreviations employed are as follows: COMU: 1-[(1-(cyano-2-ethoxy-2-oxoethylideneaminooxy)-dimethylamino-morpholinomethylene)]methanaminium hexaflourophosphate ivDde: 1-(4,4-dimethyl-2,6-dioxocyclohexylidene)3-methyl-butyl Dde: 1-(4,4-dimethyl-2,6-dioxocyclohexylidene)-ethyl DCM: dichloromethane DMF: N,N-dimethylformamide (0151) DIPEA: diisopropylethylamine EtOH: ethanol Et2O: diethyl ether HATU: N-[(dimethylamino)-1H-1,2,3-triazol[4,5-b]pyridine-1-ylmethylene]-N-methylmethanaminium hexafluorophosphate N-oxide MeCN: acetonitrile NMP: N-methylpyrrolidone (0152) TFA: trifluoroacetic acid TIS: triisopropylsilane Cleavage (0153) The resin was washed with EtOH (3×10 ml) and Et2O (3×10 ml) and dried to constant weight at room temperature (r.t.). The crude peptide was cleaved from the resin by treatment with TFA/TIS/water (95/2.5/2.5; 40 ml, 2 h; r.t.). Most of the TFA was removed at reduced pressure and the crude peptide was precipitated and washed three times with diethylether and dried to constant weight at room temperature. HPLC Purification of the Crude Peptide (0154) The crude peptide was purified to greater than 90percent by preparative reverse phase HPLC using a PerSeptive Biosystems VISION Workstation equipped with a C-18 column (5 cm; 10 mum) and a fraction collector and run at 35 ml/min with a gradient of buffer A (0.1percent TFA, aq.) and buffer B (0.1percent TFA, 90percent MeCN, aq.). Fractions were analyzed by analytical HPLC and MS and relevant fractions were pooled and lyophilized. The final product was characterized by HPLC and MS. (0155) The synthesized compounds are shown in Table 1 and Table 2

Reference： [1]Patent: US2015/299281,2015,A1 .Location in patent: Paragraph 0147-0155

45
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
[ 73731-37-0 ]
[ 96402-49-2 ]
[ 135248-89-4 ]
[ 116611-64-4 ]
Hy-CAD-[1-Nal]-VCYWHTFG-NH₂ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		Peptide monomers of the present invention were synthesized using the Merrifield solid phase synthesis techniques on Protein Technology's Symphony multiple channel synthesizer. The peptides were assembled using HBTU (0-Benzotriazole-N,N,N',N'-tetramethyl-uronium- hexafluoro-phosphate), Diisopropylethylamine(DIEA) coupling conditions. For some amino acid couplings PyAOP(7-Azabenzotriazol- 1 -yloxy)tripyrrolidinophosponium hexafluorophosphate) and DIEA conditions were used. Rink Amide MB HA resin (100-200 mesh, 0.57 mmol/g) was used for peptide with C-terminal amides and pre-loaded Wang Resin with N-a-Fmoc protected amino acid was used for peptide with C-terminal acids. The coupling reagents (HBTU and DIEA premixed) were prepared at lOOmmol concentration. Similarly amino acids solutions were prepared at 100 mmol concentration. Peptide inhibitors of the present invention were identified based on medical chemistry optimization and/or phage display and screened to identify those having superior binding and/or inhibitory properties.[00611] The peptides were assembled using standard Symphony protocols. The peptide sequences were assembled as follows: Resin (250 mg, 0.14 mmol) in each reaction vial was washed twice with 4ml of DMF followed by treatment with 2.5ml of 20percent 4-methyl piped dine (Fmoc de- protection) for lOmin. The resin was then filtered and washed two times with DMF (4ml) and re -treated with N-methyl piperifine for additional 30 minute. The resin was again washed three times with DMF (4 ml) followed by addition 2.5ml of amino acid and 2.5ml of HBTU-DIEA mixture. After 45min of frequent agitations, the resin was filtered and washed three timed with DMF (4 ml each). For a typical peptide of the present invention, double couplings were performed. After completing the coupling reaction, the resin was washed three times with DMF (4 ml each) before proceeding to the next amino acid coupling.

Reference： [1]Patent: WO2016/11208,2016,A1 .Location in patent: Paragraph 00610; 00611; 00633

46
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
[ 73731-37-0 ]
[ 96402-49-2 ]
[ 135248-89-4 ]
[ 116611-64-4 ]
Hy-CADWVCY-[1-NaI]-HTF-OH [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		Peptide monomers of the present invention were synthesized using the Merrifield solid phase synthesis techniques on Protein Technology's Symphony multiple channel synthesizer. The peptides were assembled using HBTU (0-Benzotriazole-N,N,N',N'-tetramethyl-uronium- hexafluoro-phosphate), Diisopropylethylamine(DIEA) coupling conditions. For some amino acid couplings PyAOP(7-Azabenzotriazol- 1 -yloxy)tripyrrolidinophosponium hexafluorophosphate) and DIEA conditions were used. Rink Amide MB HA resin (100-200 mesh, 0.57 mmol/g) was used for peptide with C-terminal amides and pre-loaded Wang Resin with N-a-Fmoc protected amino acid was used for peptide with C-terminal acids. The coupling reagents (HBTU and DIEA premixed) were prepared at lOOmmol concentration. Similarly amino acids solutions were prepared at 100 mmol concentration. Peptide inhibitors of the present invention were identified based on medical chemistry optimization and/or phage display and screened to identify those having superior binding and/or inhibitory properties.[00611] The peptides were assembled using standard Symphony protocols. The peptide sequences were assembled as follows: Resin (250 mg, 0.14 mmol) in each reaction vial was washed twice with 4ml of DMF followed by treatment with 2.5ml of 20percent 4-methyl piped dine (Fmoc de- protection) for lOmin. The resin was then filtered and washed two times with DMF (4ml) and re -treated with N-methyl piperifine for additional 30 minute. The resin was again washed three times with DMF (4 ml) followed by addition 2.5ml of amino acid and 2.5ml of HBTU-DIEA mixture. After 45min of frequent agitations, the resin was filtered and washed three timed with DMF (4 ml each). For a typical peptide of the present invention, double couplings were performed. After completing the coupling reaction, the resin was washed three times with DMF (4 ml each) before proceeding to the next amino acid coupling.

Reference： [1]Patent: WO2016/11208,2016,A1 .Location in patent: Paragraph 00610; 00611; 00633

47
[ 3025-95-4 ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
[ 73731-37-0 ]
[ 73724-45-5 ]
[ 135248-89-4 ]
[ 116611-64-4 ]
Hy-[β-Ala]-SCADWVCYWHTFG-OH [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		Peptide monomers of the present invention were synthesized using the Merrifield solid phase synthesis techniques on Protein Technology's Symphony multiple channel synthesizer. The peptides were assembled using HBTU (0-Benzotriazole-N,N,N',N'-tetramethyl-uronium- hexafluoro-phosphate), Diisopropylethylamine(DIEA) coupling conditions. For some amino acid couplings PyAOP(7-Azabenzotriazol- 1 -yloxy)tripyrrolidinophosponium hexafluorophosphate) and DIEA conditions were used. Rink Amide MB HA resin (100-200 mesh, 0.57 mmol/g) was used for peptide with C-terminal amides and pre-loaded Wang Resin with N-a-Fmoc protected amino acid was used for peptide with C-terminal acids. The coupling reagents (HBTU and DIEA premixed) were prepared at lOOmmol concentration. Similarly amino acids solutions were prepared at 100 mmol concentration. Peptide inhibitors of the present invention were identified based on medical chemistry optimization and/or phage display and screened to identify those having superior binding and/or inhibitory properties.[00611] The peptides were assembled using standard Symphony protocols. The peptide sequences were assembled as follows: Resin (250 mg, 0.14 mmol) in each reaction vial was washed twice with 4ml of DMF followed by treatment with 2.5ml of 20% 4-methyl piped dine (Fmoc de- protection) for lOmin. The resin was then filtered and washed two times with DMF (4ml) and re -treated with N-methyl piperifine for additional 30 minute. The resin was again washed three times with DMF (4 ml) followed by addition 2.5ml of amino acid and 2.5ml of HBTU-DIEA mixture. After 45min of frequent agitations, the resin was filtered and washed three timed with DMF (4 ml each). For a typical peptide of the present invention, double couplings were performed. After completing the coupling reaction, the resin was washed three times with DMF (4 ml each) before proceeding to the next amino acid coupling.

Reference： [1]Patent: WO2016/11208,2016,A1 .Location in patent: Paragraph 00610; 00611; 00633

48
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 112883-29-1 ]
[ 35661-40-6 ]
[ 136083-57-3 ]
[ 104091-09-0 ]
[ 71989-23-6 ]
[ 35737-15-6 ]
[ 73731-37-0 ]
[ 105047-45-8 ]
[ 73724-45-5 ]
[ 71989-20-3 ]
[ 77128-73-5 ]
[ 91000-69-0 ]
[ 116611-64-4 ]
C₁₅₀H₂₂₈N₄₀O₄₅ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: tGLP-1 and its analogues 2?13 were all synthesized using general solid-phase peptide synthesis of N-Fmoc/tBu chemistry. 63Fmoc Rink Amide-MBHA resin (0.1 mmol) was added to a 25 ml peptide synthetic vessel and swollen with DMF for 40 min. After deprotected by 25percent piperidine in DMF, a solution of Fmoc-AA-OH (0.4 mmol), HATU (0.4 mmol), HoAt (0.4 mmol) and DIPEA (0.8 mmol) in DMF was added to the vessel. After reacted for 1 h, the resin was washed three times with DMF and three times with CH2Cl2, then qualitative ninhydrin testing was performed to monitor whether some free amino groups still existed on the resin ornot. If not, the resin was washed three times with DMF again and repeated the procedures of deprotection and coupling. Forthe coupling of some unnatural amino acids, NMM instead of DIPEA and NMP instead of DMF were used. Besides, the reaction time was prolonged to 4 h. Following the final deprotection of N-terminus, the target peptide was cleaved from resin with Reagent K (TFA/thioanisole/water/phenol/EDT, 82.5:5:5:5:2.5) for 2 h atroom temperature. After filtration, the residue solution was concentrated, precipitated with cold diethyl ether and centrifuged for three times. The residue was dissolved in water and purified by Waters 2545 preparative RP-HPLC system. Sephadex G-25 was used for the further purification to remove some short peptide impurities. The molecular mass of the target peptide was confirmed by MALDI-TOF. The purity of peptide was tested with analytical RP-HPLC, and the conditions were as follows: a linear gradient of 20percent mobile phase A and 80percent mobile phase B to 80percent mobile phase A and 20percent mobile phase B (A: acetonitrile containing 0.1percent TFA; B: H2O containing 0.1percent TFA) in 30 min, at a flow rate of 1 mL/minute with UV detection at 214 nm.

Reference： [1]Bioorganic and Medicinal Chemistry,2016,vol. 24,p. 1163 - 1170

49
[ 250695-67-1 ]
[ 35661-60-0 ]
[ 112883-29-1 ]
[ 136083-57-3 ]
[ 35737-15-6 ]
[ 35661-38-2 ]
[ 73724-45-5 ]
[ 125238-99-5 ]
C₇₁H₁₁₁N₂₁O₁₈ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		1. Peptide synthesis 1.1 General synthetic procedures A general method for the synthesis of the peptidomimetics of the present invention is exemplified in the following. This is to demonstrate the principal concept and does not limit or restrict the present invention in any way. A person skilled in the art is easily able to modify these procedures, especially, but not limited to, choosing a different starting position within the ring system, to still achieve the preparation of the claimed cyclic peptidomimetic compounds of the present invention. Coupling of the first protected amino acid residue to the resin . In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1percent crosslinked; loading: 1.4 mMol/g) was swollen in dry CH2CI2 for 30 min (7 mL CH2CI2 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH2CI2/DMF (4/1) (10 mL per g resin) was added. After shaking for 2-4 h at rt the resin was filtered off and washed successively with CH2CI2, DMF, CH2CI2, DMF and CH2CI2. Then a solution of dry CH2CI2/MeOH/DIPEA (17:2:1) was added (10 mL per g resin). After shaking for 3 x 30 min the resin was filtered off in a pre-weighed sinter funnel and washed successively with CH2CI2, DMF, CH2CI2, MeOH, CH2CI2, MeOH, CH2CI2 (2x) and Et20 (2x). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control. Loading was typically 0.6 - 0.7 mMol/g. The following preloaded resins were prepared: Fmoc-Dab(Boc)-2-chlorotrityl resin, Fmoc-DDab(Boc)-2-chlorotrityl resin, Fmoc-Lys(Boc)-2-chlorotrityl resin, Fmoc- Trp(Boc)-2-chlortrityl resin, Fmoc-Phe-2-chlortrityl resin; Fmoc-Val-2-chlorotrityl resin, Fmoc-Pro-2-chlorotrityl resin, Fmoc-Arg(Pbf)-2-chlorotrityl resin and Fmoc-Glu(iBu)-2- chlorotrityl resin. Synthesis of the fully protected peptide fragment The synthesis was carried out on a Syro-peptide synthesizer (MultiSynTech GmbH) using 24 to 96 reaction vessels. In each vessel 0.04 mMol of the above resin were placed and the resin was swelled in CH2CI2 and DMF for 15 min, respectively. The following reaction cycles were programmed and carried out: Step Reagent Time 1 CH2CI2, wash and swell (manual) 1 x 3 min 2 DMF, wash and swell 2 x 30 min 3 20percent piperidine/DMF 1 x 5 min and 1 x 15 min 4 DMF, wash 5 x 1 min 5 3.5 eq Fmoc amino acid/3.5 eq HOAt in DMF + 3.5 eq PyBOP/7 eq DIPEA or 3.5 eq DIC 1 x 40 min 6 3.5 eq Fmoc amino acid/DMF + 3.5 eq HATU or PyBOP or HCTU + 7 eq DIPEA 1 x 40 min 7 DMF, wash 5 x 1 min 8 20percent piperidine/DMF 1 x 5 min and 1 x 15 min 9 DMF, wash 5 x 1 min 10 CH2CI2, wash (at the end of the synthesis) 3 x 1 min Steps 5 to 9 are repeated to add each amino-acid residue. After the termination of the synthesis of the fully protected peptide fragment, one of the procedures A - E, as described herein below, was adopted subsequently, depending on which kind of interstrand linkages, as described herein below, were to be formed. Finally, the peptides were purified by preparative reverse phase LC-MS, as described herein below. Procedure A: Cyclization and work up of a backbone cyclized peptide having no interstrand linkage Cleavage, backbone cyclization and deprotection After assembly of the linear peptide, the resin was suspended in 1 mL of 1percent TFA in CH2CI2 (v/v; 0.14 mMol) for 3 minutes. After filtration the filtrate was neutralized with 1 mL of 20percent DI PEA in CH2CI2 (v/v; 1.15 mMol). This procedure was repeated four times to ensure completion of the cleavage. An alternative cleavage method comprises suspension of the resin in lmL of 20percent HFIP in CH2CI2 (v/v; 1.9 mMol) for 30 minutes, filtration and repetition of the procedure. The resin was washed three times with 1 mL of CH2CI2. The CH2CI2 layers containing product were evaporated to dryness. The fully protected linear peptide was solubilised in 8 mL of dry DM F. Then 2 eq of HATU and 2 eq of HOAt in dry DM F (1-2 mL) and 4 eq of DIPEA in dry DM F (1-2 mL) were added to the peptide, followed by stirring for ca. 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 mL of CH2CI2 and washed three times with 4.5 mL 10percent acetonitrile in water (v/v). The CH2CI2 layer was then evaporated to dryness. To fully deprotect the peptide, 7 mL of cleavage cocktail TFA/DODT/thioanisol/H20 (87.5 :2.5:5:5) or TFA/TIS/H20 (95:2.5 :2.5) were added, and the mixture was kept for 2.5-4 h at room temperature until the reaction was completed. The reaction mixture was evaporated close to dryness, the peptide precipitated with 7 mL of cold Et20/pentane and finally washed 3 times with 4 mL of cold Et20/pentane. Procedures Bl and B2: Cyclization and work up of a backbone cyclized peptide having a disulfide interstrand linkage Bl: Formation of a disulfide interstrand linkage using DMSO After cleavage, backbone cyclization and deprotection of the linear peptide, as described in the corresponding section of procedure A, th...

Reference： [1]Patent: WO2016/50361,2016,A1 .Location in patent: Page/Page column 75-80; 86; 87

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[ 35661-60-0 ]
[ 136083-57-3 ]
[ 13734-28-6 ]
[ 91000-69-0 ]
[ 144120-53-6 ]
C₄₁H₇₅N₁₁O₁₃ [ No CAS ]