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

Uptake of L-proline by Histoplasma capsulatum

1976 ◽  
Vol 22 (8) ◽  
pp. 1188-1190 ◽  
Author(s):  
Nina Dabrowa ◽  
Dexter H. Howard
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Active Transport ◽  
Transport System ◽  
Histoplasma Capsulatum ◽  
Yeast Cells ◽  
Side Chain ◽  
Simple Diffusion ◽  
Aliphatic Side Chain ◽  
Active Transport System

The uptake and incorporation of L-proline by yeast cells of the dimorphic zoopathogen Histoplasma capsulatum were studied. The amino acid was assimilated in at least two ways: by an active transport system with a Km of 1.7 × 10−5 M and by simple diffusion. The active transport system was stereospecific and severely restricted to neutral aliphatic side-chain amino acids. Certain analogues inhibited L-proline uptake and prevented incorporation of the amino acid into cellular constituents. The inhibition of L-proline uptake by L-leucine was competitive. Since L-leucine and L-proline are seemingly transported by a system with similarcharacteristics, it must be concluded, as originally postulated, that the buckled ring of L-proline, in solution, acts as an aliphatic side chain and that this cyclic amino acid is transported by a system more or less specific for amino acids with neutral aliphatic side chains.

Reaction of amino acids with guanidinating agents

1970 ◽  
Vol 48 (11) ◽  
pp. 1189-1191 ◽  
Author(s):  
Lynn C. Allen ◽  
T. Viswanatha
Keyword(s):  
Amino Acids ◽  
Side Chain ◽  
Amino Group ◽  
Aliphatic Side Chain

The reaction of amino acids with three guanidinating agents, viz. 2-methylpseudourea, 2-methyl-2-thiopseudourea, and guanyl-3,5-dimethylpyrazole, was investigated. The α-amino group of amino acids with an aliphatic side chain was readily convertible to the guanido group. However, the α-amino group of other amino acids was found to be either refractory or slow toward such modification.

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

Redesign of (R)-Omega-Transaminase and Its Application for Synthesizing Amino Acids with Bulky Side Chain

2021 ◽  
Author(s):  
Dong-Xu Jia ◽  
Chen Peng ◽  
Jun-Liang Li ◽  
Fan Wang ◽  
Zhi-Qiang Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Side Chain ◽  
Bulky Side Chain

Vanadocene complexes of amino acids bearing functional group in the side chain

2013 ◽  
Vol 405 ◽  
pp. 121-127 ◽  
Author(s):  
Jaromír Vinklárek ◽  
Jan Honzíček ◽  
Milan Erben ◽  
Iva Klepalová ◽  
Aleš Eisner ◽  
...  
Keyword(s):  
Amino Acids ◽  
Functional Group ◽  
Side Chain

Synthesis of Alanine and Proline Amino Acids with Amino or Guanidinium Substitution on the Side Chain

Tetrahedron ◽  
2000 ◽  
Vol 56 (16) ◽  
pp. 2513-2522 ◽  
Author(s):  
Zhenyu Zhang ◽  
Arthur Van Aerschot ◽  
Chris Hendrix ◽  
Roger Busson ◽  
Frank David ◽  
...  
Keyword(s):  
Amino Acids ◽  
Side Chain
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