Amino acids and peptides. CIII. Infrared spectra and conformations of methylamides of N-acylated amino acids with a hydroxyl group in the side chain

An amino protection method was developed in which phthalic anhydride was used as the amino protection group, N,N-dimethylformamide (DMF) as solvent, L-threonine and L-serine with hydroxyl groups in side chain as the protected amino acids.The structures of products were confirmed by IR、1H NMR and 13C NMR. It is an efficient and simple protection method of amino acids with a hydroxyl group in the side chain.In addition, the synthetic method avoids the side reaction and significantly improves reaction yields(over 90%).

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Reaction of Alantolactone, an Allergenic Sesquiterpene Lactone, with some Amino Acids. Resultant Loss of Immunologic Reactivity

Canadian Journal of Biochemistry ◽

10.1139/o74-083 ◽

1974 ◽

Vol 52 (7) ◽

pp. 575-581 ◽

Cited By ~ 40

Author(s):

G. Dupuis ◽

J. C. Mitchell ◽

G. H. N. Towers

Keyword(s):

Amino Acids ◽

Contact Dermatitis ◽

Sesquiterpene Lactone ◽

Sesquiterpene Lactones ◽

Sulfhydryl Group ◽

Hydroxyl Group ◽

Side Chain ◽

Amino Group ◽

Michael Type Addition ◽

Methylene Group

A study of the reaction of a hapten, alantolactone, with some amino acids is reported. Previously, we have reported than an α-methylene group attached to the γ-lactone is the immunologic requisite of alantolactone and some other sesquiterpene lactones. Such a group is known to be capable of undergoing "Michael-type addition" with the sulfhydryl group of cysteine. We confirm this finding and report that alantolactone can also undergo addition with the imidazole group of histidine and with the ε-amino group of lysine, but not with the guanido group of arginine, the hydroxyl group of serine, or the thio ether function of methionine. We selected these amino acids for further study because of their nucleophilic side chain. Samples of alantolactone that have undergone such addition no longer produce allergic eczematous contact dermatitis, as measured by patch test.

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Ferrocenoyl conjugates of hydroxyl group containing side chain amino acids: Synthesis, electrochemical study and reactivity toward electrophiles

Journal of Organometallic Chemistry ◽

10.1016/j.jorganchem.2019.121056 ◽

2020 ◽

Vol 906 ◽

pp. 121056

Author(s):

Anas Lataifeh

Keyword(s):

Amino Acids ◽

Electrochemical Study ◽

Hydroxyl Group ◽

Side Chain

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13C nuclear magnetic resonance study of cyclodipeptides containing 13C enriched hydrophobic amino acids

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19800482 ◽

1980 ◽

Vol 45 (2) ◽

pp. 482-490 ◽

Cited By ~ 10

Author(s):

Jaroslav Vičar ◽

François Piriou ◽

Pierre Fromageot ◽

Karel Bláha ◽

Serge Fermandjian

Keyword(s):

Amino Acids ◽

Nuclear Magnetic Resonance ◽

Nuclear Magnetic Resonance Study ◽

Coupling Constants ◽

Side Chain ◽

Amino Acid Residues ◽

Magnetic Resonance Study ◽

Side Chain Conformation ◽

13C Nuclear Magnetic Resonance ◽

Hydrophobic Amino Acids

The diastereoisomeric pairs of cyclodipeptides cis- and trans-cyclo(Ala-Ala), cyclo(Ala-Phe), cyclo(Val-Val) and cyclo(Leu-Leu) containing 85% 13C enriched amino-acid residues were synthesized and their 13C-13C coupling constants were measured. The combination of 13C-13C and 1H-1H coupling constants enabled to estimate unequivocally the side chain conformation of the valine and leucine residues.

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Peptide Modifications: Versatile Tools in Peptide and Natural Product Syntheses

Synlett ◽

10.1055/s-0037-1612417 ◽

2019 ◽

Vol 30 (11) ◽

pp. 1289-1302 ◽

Cited By ~ 4

Author(s):

Phil Servatius ◽

Lukas Junk ◽

Uli Kazmaier

Keyword(s):

Amino Acids ◽

Natural Product ◽

Bond Activation ◽

Bond Formation ◽

Side Chain ◽

Peptide Backbone ◽

Claisen Rearrangements ◽

The Past ◽

Allylic Alkylations ◽

Peptide Modifications

Peptide modifications via C–C bond formation have emerged as valuable tools for the preparation and alteration of non-proteinogenic amino acids and the corresponding peptides. Modification of glycine subunits in peptides allows for the incorporation of unusual side chains, often in a highly stereoselective manner, orchestrated by the chiral peptide backbone. Moreover, modifications of peptides are not limited to the peptidic backbone. Many side-chain modifications, not only by variation of existing functional groups, but also by C–H functionalization, have been developed over the past decade. This account highlights the synthetic contributions made by our group and others to the field of peptide modifications and their application in natural product syntheses.1 Introduction2 Peptide Backbone Modifications via Peptide Enolates2.1 Chelate Enolate Claisen Rearrangements2.2 Allylic Alkylations2.3 Miscellaneous Modifications3 Side-Chain Modifications3.1 C–H Activation3.1.1 Functionalization via Csp3–H Bond Activation3.2.2 Functionalization via Csp2–H Bond Activation3.2 On Peptide Tryptophan Syntheses4 Conclusion

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