scholarly journals Stereoselectivity in Mixed Ligand Copper(II) Complexes with Electrostatic Ligand-Ligand Interactions. Application to Optical Resolution of α-Amino Acids with a Charged Side Chain

1977 ◽  
Vol 50 (7) ◽  
pp. 1776-1779 ◽  
Author(s):  
Osamu Yamauchi ◽  
Takeshi Sakurai ◽  
Akitsugu Nakahara
Keyword(s):  
Amino Acids ◽  
Optical Resolution ◽  
Mixed Ligand ◽  
Side Chain ◽  
Ligand Interactions

scholarly journals Mixed Ligand Copper(II) Complexes of α-Amino Acids with Ligand-Ligand Interactions

1976 ◽  
Vol 49 (1) ◽  
pp. 169-173 ◽  
Author(s):  
Takeshi Sakurai ◽  
Osamu Yamauchi ◽  
Akitsugu Nakahara
Keyword(s):  
Amino Acids ◽  
Mixed Ligand ◽  
Ligand Interactions

ChemInform Abstract: MIXED LIGAND COPPER(II) COMPLEXES OF α-AMINO ACIDS WITH LIGAND-LIGAND INTERACTIONS

1976 ◽  
Vol 7 (17) ◽  
pp. no-no
Author(s):  
TAKESHI SAKURAI ◽  
OSAMU YAMAUCHI ◽  
KITSUGU NAKAHARA
Keyword(s):  
Amino Acids ◽  
Mixed Ligand ◽  
Ligand Interactions

scholarly journals OPTICAL RESOLUTION OF DL-AMINO ACIDS WITH ALIPHATIC SIDE CHAIN BY USING L-PHENYLALANINE

1984 ◽  
Vol 13 (1) ◽  
pp. 113-114 ◽  
Author(s):  
Tadashi Shiraiwa ◽  
Akihiko Ikawa ◽  
Keiji Sakaguchi ◽  
Hidemoto Kurokawa
Keyword(s):  
Amino Acids ◽  
Optical Resolution ◽  
Side Chain ◽  
Aliphatic Side Chain

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

1980 ◽  
Vol 45 (2) ◽  
pp. 482-490 ◽  
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.

Peptide Modifications: Versatile Tools in Peptide and Natural Product Syntheses

Synlett ◽  
2019 ◽  
Vol 30 (11) ◽  
pp. 1289-1302 ◽  
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

Enhanced hydrate formation by natural-like hydrophobic side chain amino acids at ambient temperature: A kinetics and morphology investigation

Fuel ◽  
2021 ◽  
Vol 299 ◽  
pp. 120828
Author(s):  
Kan Jeenmuang ◽  
Chakorn Viriyakul ◽  
Katipot Inkong ◽  
Hari Prakash Veluswamy ◽  
Santi Kulprathipanja ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ambient Temperature ◽  
Hydrate Formation ◽  
Side Chain
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