(3R)-4-(1,1-Dimethylethoxy)-3-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]butanoic acid

White powder

General procedure: Solid phase peptide synthesis (0.2 mmol scale) was performed on aminomethyl PS resin (1.0 mmol/g) based on the Fmoc based strategy. HMPB linker was attached to the resin using general method A, and coupling of the first amino acid residue to theHMPB-PS resin was performed according to general method B or C. The degree of attachment of the first amino acid residue to the resin was determined using UV spectrophotometry.16 The desired peptide sequences were synthesised using general method D onTributeTM peptide synthesiser, and peptide coupling of unnatural amino acids was performed manually according to general method E. The linear peptides were cleaved from the resin using general method F, and the crude products were cyclised using general method G. The side-chain protecting groups were removed from the cyclised peptides according to general method H, and the allyl protecting group was removed according to general method I. The crude peptides were purified according to general method JGeneral procedure: Solid phase peptide synthesis (0.2 mmol scale) was performed on aminomethyl PS resin (1.0 mmol/g) based on the Fmoc based strategy. HMPB linker was attached to the resin using general method A, and coupling of the first amino acid residue to theHMPB-PS resin was performed according to general method B or C. The degree of attachment of the first amino acid residue to the resin was determined using UV spectrophotometry.16 The desired peptide sequences were synthesised using general method D onTributeTM peptide synthesiser, and peptide coupling of unnatural amino acids was performed manually according to general method E. The linear peptides were cleaved from the resin using general method F, and the crude products were cyclised using general method G. The side-chain protecting groups were removed from the cyclised peptides according to general method H, and the allyl protecting group was removed according to general method I. The crude peptides were purified according to general method JGeneral procedure: Solid phase peptide synthesis (0.2 mmol scale) was performed on aminomethyl PS resin (1.0 mmol/g) based on the Fmoc based strategy. HMPB linker was attached to the resin using general method A, and coupling of the first amino acid residue to theHMPB-PS resin was performed according to general method B or C. The degree of attachment of the first amino acid residue to the resin was determined using UV spectrophotometry.16 The desired peptide sequences were synthesised using general method D onTributeTM peptide synthesiser, and peptide coupling of unnatural amino acids was performed manually according to general method E. The linear peptides were cleaved from the resin using general method F, and the crude products were cyclised using general method G. The side-chain protecting groups were removed from the cyclised peptides according to general method H, and the allyl protecting group was removed according to general method I. The crude peptides were purified according to general method JGeneral procedure: Solid phase peptide synthesis (0.2 mmol scale) was performed on aminomethyl PS resin (1.0 mmol/g) based on the Fmoc based strategy. HMPB linker was attached to the resin using general method A, and coupling of the first amino acid residue to theHMPB-PS resin was performed according to general method B or C. The degree of attachment of the first amino acid residue to the resin was determined using UV spectrophotometry.16 The desired peptide sequences were synthesised using general method D onTributeTM peptide synthesiser, and peptide coupling of unnatural amino acids was performed manually according to general method E. The linear peptides were cleaved from the resin using general method F, and the crude products were cyclised using general method G. The side-chain protecting groups were removed from the cyclised peptides according to general method H, and the allyl protecting group was removed according to general method I. The crude peptides were purified according to general method JGeneral procedure: Solid phase peptide synthesis (0.2 mmol scale) was performed on aminomethyl PS resin (1.0 mmol/g) based on the Fmoc based strategy. HMPB linker was attached to the resin using general method A, and coupling of the first amino acid residue to theHMPB-PS resin was performed according to general method B or C. The degree of attachment of the first amino acid residue to the resin was determined using UV spectrophotometry.16 The desired peptide sequences were synthesised using general method D onTributeTM peptide synthesiser, and peptide coupling of unnatural amino acids was performed manually according to general method E. The linear peptides were cleaved from the resin using general method F, and the crude products were cyclised using general method G. The side-chain protecting groups were removed from the cyclised peptides according to general method H, and the allyl protecting group was removed according to general method I. The crude peptides were purified according to general method J

Molecular Weight:397.5
XLogP3:3.5
Hydrogen Bond Donor Count:2
Hydrogen Bond Acceptor Count:5
Rotatable Bond Count:9
Exact Mass:397.18892296
Monoisotopic Mass:397.18892296
Topological Polar Surface Area:84.9
Heavy Atom Count:29
Complexity:550
Defined Atom Stereocenter Count:1
Covalently-Bonded Unit Count:1
Compound Is Canonicalized:Yes