Synthetic homo‐oligomethionine chemoattractants

Bismara, C.; Bonora, Gian Maria; Toniolo, Claudio; Becker, Elmer L.; Freer, Richard J.

doi:10.1111/j.1399-3011.1985.tb01015.x

Cited by 10 publications

(2 citation statements)

References 21 publications

(5 reference statements)

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“…This observation emphasizes the importance of this group, which has been shown to be important in the formation of the peptide/receptor complex (25,26). First, the implication of the CO (formyl) into intramolecular H-bonds is shown to be the main conformational difference between normal and thiopeptides.…”

Section: Mlp-otrumentioning

confidence: 79%

Crystal and molecular structure of two geometrically restricted chemotactic tripeptides, analogues of formyl‐methionine‐leucine‐phenylalanine*

Michel

Lajoie

Hassani³

1990

International Journal of Peptide and Protein Research

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The crystal structures of HCO-Met-Leu-Phe-OC(CH,), , (CH2,H3,NjO5S), fMLP-OtBu, and HCO-Met$ [CSNHI-Leu-Phe-OCH,, (C22H33 N,O,Sz), f M s LP-OMe, have been determined by single crystal X-ray diffraction, and their conformational properties investigated by molecular mechanics energy calculations. Crystals of fMLP-OtBu are monoclinic, space group P2,, a = 12.027(4), b = 9.492(3), c = 12.660(4)A, = 101.99(3)", Z = 2; those of fM'LP-OMe are orthorhombic, space group P21212,, a = 7.130(1), b = 12.097(2), c = 31.060(5) A, Z = 4 . The first compounds f M L P -0 t h is the t-butyl esterof the tripeptide f M L P that represents one of the most potent compounds in inducing the lysozyme release from human neutrophils that reflects the chemotactic activity. From the crystal structure, it is shown that the orientation of the phenylalanine side chain is largely affected by the presence of the bulky group. fMs LP-OMe was shown to be inactive after thionation of the methionine residue in the original tripeptide.Nevertheless, the crystal structure does not reveal any influence of the presence of the thionated peptidic bond on the backbone conformation. The X-ray results have been used to generate parameters for empirical energy calculations. Subsequently, a strategy based on random generation of conformations followed by energy-minimization was applied to investigate the conformational space of thiopeptides, in comparison with normal peptides. From molecular free energy calculations, it is shown that the main influence of the introduction of a thioamide bond on the molecular structure is to prevent the existence of C&onformations involving the thiomethionine residue. Consequently, a larger number of conformers are found to form intramolecular hydrogen bonds involving the formyl group, reducing its availability to interact with the receptor. For the first time, the theoretical prediction of the existence of C,& conformations for f M L P is made. The resulting conformers are compared to previously active structures of these chemotactic agents.

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Section: Mlp-otrumentioning

confidence: 79%

Crystal and molecular structure of two geometrically restricted chemotactic tripeptides, analogues of formyl‐methionine‐leucine‐phenylalanine*

Michel

Lajoie

Hassani³

1990

International Journal of Peptide and Protein Research

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“…This result is in perfect agreement with the literature which emphasizes the importance of the availability of these two groups in the formation of the substrate-receptor complex. 7,16,39,[47][48][49][50][51][52][53][54] The determination of the native structure of the fMLP analogs can be deduced by comparing the conformational preferences of the two tripeptides for the conformers that we have presented in Table1 and Table 2.…”

Section: Discussionmentioning

confidence: 99%

Structural Requirements for Molecular Recognition by fMLP Analogs Receptors: Comparative Conformational Analysis of (for-Met-Leu-Phe-OMe) and its Thioamide Analog (for-Met-Leuψ[CSNH]Phe-OMe)

Hassani

Houssat

Hazm

et al. 2018

ACSi

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In order to determine the structural requirements of fMLP analogs receptors, this work presents the results of a comparative conformational analysis of the active chemotactic peptide (formyl-Met-Leu-Phe-OMe) and its inactive analog (formyl-Met-Leuψ [CSNH] Phe-OMe) using the theoretical method PEPSEA. This study showed that a γ turn structure centered on the central residue is the native structure of the chemotactic peptide fMLP analogs, where both CO(formyl) and NH(central residue) groups are available and ready to interact with the receptor. The inactive analog fML S P-OMe prefers instead a γ turn structure centered on the Met residue, where the two groups cited above are not available for this interaction. Our results and those of literature enable us to propose the "induced fit" model of Burgen for the molecular recognition process. Consequently, the activity of fMLP analogs chemotactic peptides would not be related to a specific secondary structure (β turn, γ turn or extended….) but rather to the freedom and the availability of the CO(formyl) and the NH group at position 2.

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Physical Data of Oligomers

Rothe

1999

The Wiley Database of Polymer Properties

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Synthetic homo‐oligomethionine chemoattractants

Cited by 10 publications

References 21 publications

Crystal and molecular structure of two geometrically restricted chemotactic tripeptides, analogues of formyl‐methionine‐leucine‐phenylalanine*

Crystal and molecular structure of two geometrically restricted chemotactic tripeptides, analogues of formyl‐methionine‐leucine‐phenylalanine*

Structural Requirements for Molecular Recognition by fMLP Analogs Receptors: Comparative Conformational Analysis of (for-Met-Leu-Phe-OMe) and its Thioamide Analog (for-Met-Leuψ[CSNH]Phe-OMe)

Physical Data of Oligomers

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