(R)-N-Fmoc-4-Bromophenylalanine

white to off-white powder

General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.General procedure: 350 mg of the beads (1.0 x 106 beads) were split equally to distribute into15 reaction vessels and the beads in each reaction vessel (23 mg, 6.6 x 104 beads) was treated with 6 equivalent ofFmoc-aa-OH (36 mumol), 6 equivalent of Oxyma (36 mumol, 5.1 mg), and 6 equivalent of DIC (36 mumol, 5.7 muL) in 182muL of DMF subjected to coupling of one of the following 15 amino acids; Fmoc-D-Ala-OH, Fmoc-D-Asp-OH, Fmoc-D-Glu-OH, Fmoc-D-Phe-OH, Fmoc-D-His(Trt)-OH, Fmoc-D-Lys(Boc)-OH, Fmoc-D-Leu-OH, Fmoc-D-Asn(Trt)-OH, Fmoc-D-Gln(Trt)-OH, Fmoc-D-Ser(OtBu)-OH, Fmoc-D-Thr(OtBu)-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. The coupling reaction was carried out at RT for2-4 h with gentle shaking. The beads were washed with DMF three times. The beads were pooled and mixed. Fmocgroup was deprotected by exposing resin to 20% piperidine in DMF. First resin was treated with 20% piperidine in DMFfor 3 min then with fresh 20% piperidine in DMF for 12 min. The beads were washed with DMF three times. Thisprocedure of split, coupling, mix, and Fmoc deprotection was repeated 12 times to synthesize 12-mer random peptides.For X3, X7, X11 residues, beads were split into 7 reaction vessels and the following seven amino acids, instead of theabovementioned 15 remino acids, were used for coupling; Fmoc-D-Ala-OH, Fmoc-D-Phe-OH, Fmoc-D-Leu-OH, Fmoc-D-Val-OH, Fmoc-D-Trp(Boc)-OH, Fmoc-D-Tyr(OtBu)-OH, and Fmoc-Aib-OH. After completion of the 12thresidue, beads were mixed and stored at -20 C.

Molecular Weight:466.3
XLogP3:5.3
Hydrogen Bond Donor Count:2
Hydrogen Bond Acceptor Count:4
Rotatable Bond Count:7
Exact Mass:465.05757
Monoisotopic Mass:465.05757
Topological Polar Surface Area:75.6
Heavy Atom Count:30
Complexity:584
Defined Atom Stereocenter Count:1
Covalently-Bonded Unit Count:1
Compound Is Canonicalized:Yes