Side-chain interactions between sulfur-containing amino acids and phenyalanine in .alpha.-helixes

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

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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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Model studies regarding the internal corrosion of tin-plated food cans. III. Binding of tin(II) ions and iron(II) ions by sulfur-containing amino acids

Journal of Agricultural and Food Chemistry ◽

10.1021/jf60186a015 ◽

1973 ◽

Vol 21 (2) ◽

pp. 246-251 ◽

Cited By ~ 4

Author(s):

Dieter W. Gruenwedel ◽

Hsien-Chung Hao

Keyword(s):

Amino Acids ◽

Internal Corrosion ◽

Model Studies ◽

Sulfur Containing

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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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