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1.  Synthesis of dehydrodipeptide esters and their evaluation as inhibitors of cathepsin C 
Medicinal Chemistry Research  2015;24(8):3157-3165.
The procedures for the synthesis of esters of dehydropeptides containing C-terminal (Z)-dehydrophenylalanine and dehydroalanine have been elaborated. These esters appeared to be moderate or weak inhibitors of cathepsin C, with some of them exhibiting slow-binding behavior. As shown by molecular modeling, they are rather bound at the surface of the enzyme and are not submersed in its binding cavities.
Electronic supplementary material
The online version of this article (doi:10.1007/s00044-015-1366-0) contains supplementary material, which is available to authorized users.
doi:10.1007/s00044-015-1366-0
PMCID: PMC4500854  PMID: 26190908
Dehydropeptides; Esterification; Enzyme inhibitors; Molecular modeling
2.  Crystal structure of N-(tert-but­oxy­carbon­yl)phenyl­alanylde­hydro­alanine isopropyl ester (Boc–Phe–ΔAla–OiPr) 
In the crystal structure of the de­hydro­dipeptide (Boc-Phe-ΔAla-OiPr), the mol­ecule has a trans configuration of the N-methyl­amide group. Its geometry is different from saturated peptides but is in excellent agreement with other de­hydro­alanine compounds. In the crystal, an N—H⋯O hydrogen bond links the mol­ecules in a herringbone packing arrangement.
In the title compound, the de­hydro­dipeptide (Boc–Phe–ΔAla–OiPr, C20H28N2O5), the mol­ecule has a trans conformation of the N-methyl­amide group. The geometry of the de­hydro­alanine moiety is to some extent different from those usually found in simple peptides, indicating conjugation between the H2C=C group and the peptide bond. The bond angles around de­hydro­alanine have unusually high values due to the steric hindrance, the same inter­action influencing the slight distortion from planarity of the de­hydro­alanine. The mol­ecule is stabilized by intra­molecular inter­actions between the isopropyl group and the N atoms of the peptide main chain. In the crystal, an N—H⋯O hydrogen bond links the mol­ecules into ribbons, giving a herringbone head-to-head packing arrangement extending along the [100] direction. In the stacks, the mol­ecules are linked by weak C—H⋯O hydrogen-bonding associations.
doi:10.1107/S1600536814025197
PMCID: PMC4257372  PMID: 25553003
crystal structure; de­hydro peptides; α,β-de­hydro­amino acids; de­hydro­alanine; herringbone packing
3.  Crystal structure of N-(tert-but­oxy­carbon­yl)glycyl-(Z)-β-bromo­dehydro­alanine methyl ester [Boc–Gly–(β-Br)(Z)ΔAla–OMe] 
In a de­hydro­amino acid with a C=C bond between the α- and β-C atoms, the amino acid residues are linked trans to each other and there are no strong intra­molecular hydrogen bonds. The torsion angles indicate a non-helical conformation of the mol­ecule.
The title compound, C11H17BrN2O5, is a de­hydro­amino acid with a C=C bond between the α- and β-C atoms. The amino acid residues are linked trans to each other and there are no strong intra­molecular hydrogen bonds. The torsion angles indicate a non-helical conformation of the mol­ecule. The dipeptide folding is influenced by an inter­molecular N—H⋯O hydrogen bond and also minimizes steric repulsion. In the crystal, mol­ecules are linked by strong N—H⋯O hydrogen bonds, generating (001) sheets. The sheets are linked by weak C—H⋯O and C—H⋯Br bonds and short Br⋯Br [3.4149 (3) Å] inter­actions.
doi:10.1107/S1600536814025677
PMCID: PMC4257433  PMID: 25553002
crystal structure; β-bromo­dehydro­alanine; de­hydro­amino acid; non-helical conformation; hydrogen bonding
4.  Two penta­dehydro­peptides with different configurations of the ΔPhe residues 
Comparison of the crystal structures of two penta­dehydro­peptides containing ΔPhe residues, namely (Z,Z)-N-(tert-butoxy­carbonyl)­glycyl-α,β-phenyl­alanyl­glycyl-α,β-phenyl­alanyl­glycine (or Boc0–Gly1–ΔZPhe2–Gly3–ΔZPhe4–Gly5–OH) methanol solvate, C29H33N5O8·CH4O, (I), and (E,E)-N-(tert-butoxy­carbonyl)­glycyl-α,β-phenyl­alanyl­glycyl-α,β-phenyl­alanyl­glycine (or Boc0–Gly1–ΔEPhe2–Gly3–ΔEPhe4–Gly5–OH), C29H33N5O8, (II), indicates that the ΔZPhe residue is a more effective inducer of folded structures than the ΔEPhe residue. The values of the torsion angles ϕ and ψ show the presence of two type-III′ β-turns at the ΔZPhe residues and one type-II β-turn at the ΔEPhe residue. All amino acids are linked trans to each other in both peptides. β-Turns present in the peptides are stabilized by intra­molecular 4→1 hydrogen bonds. Mol­ecules in both structures form two-dimensional hydrogen-bond networks parallel to the (100) plane.
doi:10.1107/S0108270110003094
PMCID: PMC2855584  PMID: 20203407

Results 1-4 (4)