Cholecystokinin Heptapeptide Analogues with Multiple Modification in Peptide Chain

Hlaváček, Jan; Pírková, Jana; Žertová, Miroslava; Pospíšek, Jan; Maletı́nská, Lenka; Slaninová, Jiřina

doi:10.1135/cccc19932761

Collect. Czech. Chem. Commun.

1993

DOI: 10.1135/cccc19932761

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Cholecystokinin Heptapeptide Analogues with Multiple Modification in Peptide Chain

Jan Hlaváček

Jana Pírková

Miroslava Žertová

et al.

Abstract: Using solid phase synthesis we prepared the cholecystokinin fragment Boc-CCK-7 (Boc-Tyr(SO3-Na+)-Met-Gly-Trp-Met-Asp-Phe-NH2) Ia and its seven analogues Ib - Ih. In the analogues Ib and Ic the Met residue in the carboxyterminal part of the molecule was substituted for L- or D-Phe Me3. In the analogues Id and Ie with Phe residue substituted by L- or D-Phe Me3 the Neo was inserted in the place of this Met residue and in the analogues If and Ig, an addition to PheMe3 substitution in the carboxyterminus, both Met … Show more

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“…Peptidomimetics with some of these modified side chains have been synthesized and incorporated in the design of numerous drug candidates (30)(31)(32)(33)(34)(35)(36)(37). Contour thickness decreases as its value relative to the global minimum increases.…”

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Conformational studies on model dipeptides of Gly, L ‐Ala and their C^α‐substituted analogs

Ramnarayan¹,

Chan²,

Balaji³

et al. 1995

International Journal of Peptide and Protein Research

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As a part of the development of conformational guidelines for the design of metabolically altered peptidomimetics, we present conformational energy calculations on model dipeptide compounds with glycine (Gly), L-alanine (Ala), r-aminoisobutyric acid (Aib), L-terr-butylglycine (Tle), L-phenylglycine (Phg), (.,a)diphenylglycine (Dqg), L-2-aminobutyric acid (Abu), 2-amino-2-ethylbutync acid (Deg), ~-2-amino-2vinylacetic acid (Ava) and (%,a)-divinylglycine (Dvg). The energy calculations have been made using molecular mechanics methods with a force field derived from MM2. The salient features are expressed in terms of conformational energy plots, drawn as a function of the backbone torsion angles $(Ci-1-Ni-C;-CI) and $(Ni-C;-CLN, + 1). The low-energy structures of these compounds are qualitatively consistent with the X-ray crystal structure analyses of peptides and peptidomimetics. They are also in agreement with the results of the solution-phase studies carried out by NMR and IR techniques. The results obtained have important implications in the design of conformationally restricted peptidomimetics. 0 Munksgaard 1995.

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confidence: 99%

Conformational studies on model dipeptides of Gly, L ‐Ala and their C^α‐substituted analogs

Ramnarayan¹,

Chan²,

Balaji³

et al. 1995

International Journal of Peptide and Protein Research

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Utilization of some non coded amino acids as isosters of peptide building blocks

et al. 1996

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In our study on non coded amino acids and their utilization in peptide chemistry we synthesized methylene-thio (CH2-S) and methyleneoxy (CH2-O) group containing amino acids and pseudodipeptides which could be used as building blocks for the construction of peptide hormone analogues. The (CH2-S) isoster of peptide bond exhibits increased flexibility, lipophility and resistance to proteolytic enzymes. This group exhibits similar properties as the isosteric disulfide bond in the side chain of cystine residue. The (CH2-O) isoster is moreover similar in its geometry to extended conformation of peptide bond. As a consequence, the changed profile of biological activities could be expected for peptide hormone analogues containing such isosteric moiety. The (CH2-S) isosters of the peptide bond were prepared by alkylation of thiolates of 2-mercaptocarboxylic acids, the disulfide bond by alkylation of cysteine or homocysteine. The (CH2-O) isosters were prepared by (AcO)4Rh2 catalyzed addition of carbenes of alkyl diazocarboxylates to N-protected aminoalcohols. Pseudodipeptides H-Leu-ψ(CH2-S)-Gly-NH2 and H-Leu-ψ(CH2-O)-Gly-NH2 were introduced into the C-terminal part of the oxytocin molecule using solution methods of peptide chemistry. Both inserted isosteric bonds were resistant against proteolytic degradation, the first one was found to decrease an enzymic cleavage of the distant Tyr(2)-Ile(3) bond in the corresponding analogue, too. The (CH2-S) isosters of the disulfide bond containing an orthogonal protection of theirα-amino (Fmoc) andα-(OAll, OH) orω-(OBu(+), OH) carboxylic groups were applied in the solid phase synthesis of the aminoterminal 1-deamino-15-pentadecapeptide of endothelin-I which represents a strong vasoactive agent. The solid phase synthesis was carried out by the step-wise protocol on the Rink or Merrifield type resin using orthogonally protected carba cystine building blocks.

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A unified approach to mesityl amino acids based on Sharpless dihydroxylation

Ramón¹,

Alonso²,

Riéra³

2007

Tetrahedron: Asymmetry

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Cholecystokinin Heptapeptide Analogues with Multiple Modification in Peptide Chain

Cited by 3 publications

References 0 publications

Conformational studies on model dipeptides of Gly, L ‐Ala and their C^α‐substituted analogs

Conformational studies on model dipeptides of Gly, L ‐Ala and their C^α‐substituted analogs

Utilization of some non coded amino acids as isosters of peptide building blocks

A unified approach to mesityl amino acids based on Sharpless dihydroxylation

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Cholecystokinin Heptapeptide Analogues with Multiple Modification in Peptide Chain

Cited by 3 publications

References 0 publications

Conformational studies on model dipeptides of Gly, L ‐Ala and their Cα‐substituted analogs

Conformational studies on model dipeptides of Gly, L ‐Ala and their Cα‐substituted analogs

Utilization of some non coded amino acids as isosters of peptide building blocks

A unified approach to mesityl amino acids based on Sharpless dihydroxylation

Contact Info

Product

Resources

About

Conformational studies on model dipeptides of Gly, L ‐Ala and their C^α‐substituted analogs

Conformational studies on model dipeptides of Gly, L ‐Ala and their C^α‐substituted analogs