OCTADECANEDIOIC ACID MONO-TERT-BUTYL ESTER

To a 50mL three-necked flask were added 1.0g compound BP103n00 (1.0eq, wherein eq represents the equavilent, the same below), 10ml dichloromethane, 10ml tert-butanol, 0.40g DIC(1.0eq), and 0.39g DMAP (1.0eq, 4-dimethylaminopyridine). They were stirred overnight at room temperature, monitored by TLC (thin-layer chromatography) until the completion of the reaction, diluted with ether, and then washed with water for 3 times, washed with saturated brine, dried over anhydrous sodium sulfate, and chromatographed in a column to give 10.4g BP103n0 as a foamy powder.A suspension of octadecanedioic acid (15 g, 47.7 mmol) in Toluene (191 ml) was brought to reflux in 3 neck 1 L round bottom flask. When all of the acid was in solution, 1, 1 -di-tert-butoxy-N, N-dimethylmethanamine (22.87 ml, 95 mmol) wasadded dropwise over 30 minutes. The reaction mixture was heated under reflux overnight. The reaction was stopped after 20 total hours of heating. The reaction mixture was cooled to room temperature resulting in precipitation of solids. The mixture was filtered by vacuum filtration. The resulting white solid was suspended in 200 ml dichloromethane and stirred for 15 minutes. The remaining solids wereremoved via vacuum filtration. The collected solids were again suspended in dichloromethane and stirred for 15 minutes. After a second filtration the combined filtrates were concentrated in vacuo and the resulting white powder was dried undervacuum. 18-(tert-butoxy)-18-oxooctadecanoic acid (10.14 g, 27.4 mmol, 57.4 percent yield) was isolated as a white solid. ‘H NMR (400MHz, CHLOROFORM-d) ö 2.35(t, J=7.5 Hz, 2H), 2.21 (t, J=7.5 Hz, 2H), 1.70 - 1.52 (m, 4H), 1.45 (s, 9H), 1.36 -1.22 (m, 24H).General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.General procedure: General method for preparation of the peptide and introduction of the substituent The preparation of the peptide was carried out with SPPS using Fmoc based chemistry on a Prelude Solid Phase Peptide Synthesizer from Protein Technologies (Tucson, AZ 85714 U.S.A.). The Fmoc-protected amino acids used in the methods were the standard recommended : Fmoc-Ala-OH, Fmoc-Arg(Pbf)-OH, Fmoc- Asn(Trt)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Cys(Trt)-OH, Fmoc-Cys(Mmt)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Glu(OtBu)-OH, Fmoc-Gly-OH, Fmoc-His(Trt)-OH, Fmoc- Ile-OH, Fmoc-Leu-OH, Fmoc-Lys(Boc)-OH, Boc-Lys(Fmoc)-OH Fmoc-Phe-OH, Fmoc-Pro-OH, Fmoc-Ser(tBu)-OH, Fmoc-Thr(tBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc- Tyr(tBu)-OH, Fmoc-Val-OH and Fmoc-Lys(Mtt)-OH supplied from e.g. Anaspec, Bachem, Iris Biotech or NovabioChem. A Wang resin preloaded with an amino acid such as Fmoc-Phe-Wang resin or the like was used (for derivatives containing Nphe, 4-CI-Nphe, or alpha-Me-Phe, a 2-Chlorotrityl resin was used). Fmoc- deprotection was achieved with 20% piperidine in NMP. Peptide couplings were performed by using DIC/Oxyma Pure with collidine. Amino acid/Oxyma Pure solutions (0.3 M/0.3 M in DMF at a molar excess of 3-10 fold) was added to the resin followed by the same molar equivalent of DIC (3 M in NMP) followed by collidine (3 M in NMP). Fmoc-Cys(Trt)-OH was used for peptides prepared for methylene bridge introduction according to method A, while Fmoc-Cys(Mmt)-OH was used for peptides prepared for methylene bridge introduction according to method B.

Molecular Weight:370.6
XLogP3:7.7
Hydrogen Bond Donor Count:1
Hydrogen Bond Acceptor Count:4
Rotatable Bond Count:19
Exact Mass:370.30830982
Monoisotopic Mass:370.30830982
Topological Polar Surface Area:63.6
Heavy Atom Count:26
Complexity:358
Covalently-Bonded Unit Count:1
Compound Is Canonicalized:Yes