Synthesis, properties and crystal structure of the tripeptide boc-L-prolyl-L-propargylglycyl-glycine methylester

Willisch, Hans; Hiller, W.; Hemmasi, Bahram; Bayer, Ernst

doi:10.1016/s0040-4020(01)86435-8

Cited by 7 publications

(6 citation statements)

References 16 publications

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“…Three model peptides in Table VI do not adopt the @-folded structure either because of the cis disposition of the Boc-Pro amide bond in Boc-Pro-Ser-NHMe69 and Boc-Pro-Pra-Gly-OMe, 75 or of a very strong side chain to peptide carbonyle interaction in Piv-Pro-His'-NHMe (Figure 12b), whereas the His NH is in close contact with the PF; anion.74 This last derivative, compared with the neutral Piv-Pro-His-NHMe (Figure 12a), illustrates the influence of the ionic state of the side chain in the conformational properties of the peptides.…”

Section: Figure 13mentioning

confidence: 99%

Crystal structures of peptides and modified peptides

Marraud

Aubry

1996

Biopolymers

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The X‐ray diffraction experiments on peptides and related molecules which have been carried out in Western Europe, except Italy, in the last eight years are reviewed. The crystal structures of some bioactive peptides such as Leu‐enkephalin (a neurotransmitter), cyclosporin A (an immunomodulator in both the free and protein‐bound state), balhimycin (an antibiotic) and octreotide (a somatostatin analogue) are briefly presented. Crystallized N‐ and C‐protected model peptides have given an insight into the folding tendency and folding modes depending on the peptide sequences. The crystal structures of various pseudopeptide molecules reveal how the three‐dimensional structure of peptide analogues can be modulated by substituting non‐peptide groups for the peptide bond. A few examples of structural mimetics of the β‐ and γ‐turns, and of templates for α‐helix induction are also presented. © 1996 John Wiley & Sons, Inc.

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Section: Figure 13mentioning

confidence: 99%

Crystal structures of peptides and modified peptides

Marraud

Aubry

1996

Biopolymers

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“…The helical tendencies of Aib have been well characterized by numerous experimental and theoretical studies of short peptides that form 3 10 -helices and longer helices that form mixed 3 10 /α-helices and αhelices. ,− On the other hand, cycloaliphatic residues (Figure ), abbreviated Ac n c, have shown a great conformational versatility. Thus, peptides containing Ac n c residues have been recently investigated by both experimental and theoretical methods. − The three-membered ring Ac 3 c shows a remarkable preference for the “bridge” region of the conformational space (φ,ψ = ±90°,0°) that can be accommodated in β-bends and in 3 10 -helices. On the contrary, the less strained residues Ac n c with n > 3 display a conformational behavior similar to that of Aib.…”

Section: Introductionmentioning

confidence: 99%

Conformational Properties of α-Amino Acids Disubstituted at the α-Carbon

Alemán

1997

J. Phys. Chem. B

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The conformational preferences of dipeptides from α-aminoisobutyric acid (Aib), 1-aminocyclopropane-1-carboxylic acid (Ac3c), and 1-aminocyclobutane-1-carboxylic acid (Ac4c) residues have been determined by ab initio quantum mechanical calculations. The results obtained evidence for the intrinsic helix-forming tendency of the Aib residue. Furthermore, the conformational preferences of Ac3c and Ac4c dipeptides are reported and the differences explained in terms of the size of their cyclic side chains. Finally, the large number of minima characterized for these conformationally restricted residues is explained as a function of the deformability of the molecular geometries.

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“…1-Aminocyclopentane-1-carboxylic acid (Ac 5 c) (Toniolo 1989; Crisma et al 1988;Santini et al 1988;Perczel et al 1991;Willisch et al 1991;Barazza et al 2005) was introduced in analogue X. Ac 5 c has a greater propensity to induce a helical conformation than Aib in the N-terminal position and this was confirmed by studies on the TOAC residue (Bui et al 2000). As previously observed (Barazza et al 2005), analogue X has a high a-helix content (Fig.…”

Section: Resultsmentioning

confidence: 62%

Design, conformational studies and analysis of structure–function relationships of PTH (1–11) analogues: the essential role of Val in position 2

et al. 2011

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The N-terminal 1-34 segment of parathyroid hormone (PTH) is fully active in vitro and in vivo and it elicits all the biological responses characteristic of the native intact PTH. Recent studies reported potent helical analogues of the PTH (1-11) with helicity-enhancing substitutions. This work describes the synthesis, biological activity, and conformational studies of analogues obtained from the most active non-natural PTH (1-11) peptide H-Aib-Val-Aib-Glu-Ile-Gln-Leu-Nle-His-Gln-Har-NH2; specifically, the replacement of Val in position 2 with D-Val, L-(αMe)-Val and N-isopropyl-Gly was studied. The synthesized analogues were characterized functionally by in-cell assays and their structures were determined by CD and NMR spectroscopy. To clarify the relationship between the structure and activity, the structural data were used to generate a pharmacophoric model, obtained overlapping all the analogues. This model underlines the fundamental functional role of the side chain of Val2 and, at the same time, reveals that the introduction of conformationally constrained Cα-tetrasubstituted α-amino acids in the peptides increases their helical content, but does not necessarily ensure significant biological activity.

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Synthesis, properties and crystal structure of the tripeptide boc-L-prolyl-L-propargylglycyl-glycine methylester

Cited by 7 publications

References 16 publications

Crystal structures of peptides and modified peptides

Crystal structures of peptides and modified peptides

Conformational Properties of α-Amino Acids Disubstituted at the α-Carbon

Design, conformational studies and analysis of structure–function relationships of PTH (1–11) analogues: the essential role of Val in position 2

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