ChemInform Abstract: Synthesis and Biological Activity of Branched Enkephalin Analogues Containing Two Amino Acids in a Side Chain

ChemInform ◽  
2010 ◽  
Vol 29 (36) ◽  
pp. no-no
Author(s):  
I. BOBROVA ◽  
N. MISHLAKOVA ◽  
A. SELANDER ◽  
E. MEKSHUN ◽  
G. ROZENTAL
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Side Chain ◽  
Enkephalin Analogues

Synthesis and biological activity of branched enkephalin analogues containing two amino acids in a side chain

1998 ◽  
Vol 33 (4) ◽  
pp. 331-334 ◽  
Author(s):  
Irina Bobrova ◽  
Natalia Mishlakova ◽  
Anette Selander ◽  
Elena Mekshun ◽  
Guntis Rozental
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Side Chain ◽  
Enkephalin Analogues

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.

Synthesis and biological activity of new metallocenic angiotensin II analogs

1988 ◽  
Vol 53 (11) ◽  
pp. 2914-2919 ◽  
Author(s):  
Pierrette Maes ◽  
Annie Ricouart ◽  
Emmanuel Escher ◽  
André Tartar ◽  
Christian Sergheraert
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Angiotensin Ii ◽  
Solid Phase ◽  
Rabbit Aorta ◽  
Phase Method ◽  
Solid Phase Method

Analogs of angiotensin II in which phenylalanine in position 8 was replaced with cymantrenylalanine or with its triphenylphosphine photosubstitution product were synthesized by the solid-phase method. On rabbit aorta strips, these peptides were found to be pure antagonists of angiotensin II. Their relative affinities are higher than most other analogs substituted in position 8 with bulky amino-acids.

scholarly journals Synthesis and Biological Activity of Brassinosteroid Analogues with a Nitrogen-Containing Side Chain

2020 ◽  
Vol 22 (1) ◽  
pp. 155
Author(s):  
Mikhail V. Diachkov ◽  
Karoll Ferrer ◽  
Jana Oklestkova ◽  
Lucie Rarova ◽  
Vaclav Bazgier ◽  
...  
Keyword(s):  
Biological Activity ◽  
Functional Groups ◽  
Side Chain ◽  
Biotic And Abiotic Stresses ◽  
Short Side ◽  
Arabidopsis Root ◽  
Physiological Processes ◽  
Growth Promoting ◽  
The Impact ◽  
Brassinosteroid Analogues

Brassinosteroids are a class of plant hormones that regulate a broad range of physiological processes such as plant growth, development and immunity, including the suppression of biotic and abiotic stresses. In this paper, we report the synthesis of new brassinosteroid analogues with a nitrogen-containing side chain and their biological activity on Arabidopis thaliana. Based on molecular docking experiments, two groups of brassinosteroid analogues were prepared with short and long side chains in order to study the impact of side chain length on plants. The derivatives with a short side chain were prepared with amide, amine and ammonium functional groups. The derivatives with a long side chain were synthesized using amide and ammonium functional groups. A total of 25 new brassinosteroid analogues were prepared. All 25 compounds were tested in an Arabidopsis root sensitivity bioassay and cytotoxicity screening. The synthesized substances showed no significant inhibitory activity compared to natural 24-epibrassinolide. In contrast, in low concentration, several compounds (8a, 8b, 8e, 16e, 22a and 22e) showed interesting growth-promoting activity. The cytotoxicity assay showed no toxicity of the prepared compounds on cancer and normal cell lines.

scholarly journals Relationship of 25-hydroxyvitamin D3 side chain structure to biological activity.

1975 ◽  
Vol 250 (1) ◽  
pp. 226-230
Author(s):  
M F Holick ◽  
M Garabedian ◽  
H K Schnoes ◽  
H F DeLuca
Keyword(s):  
Biological Activity ◽  
Chain Structure ◽  
Side Chain ◽  
Relationship Of

Replacement of the interchain disulfide bridge-forming amino acids A7 and B7 by glutamate impairs the structure and activity of insulin

2004 ◽  
Vol 385 (12) ◽  
pp. 1171-1175 ◽  
Author(s):  
Zhan-Yun Guo ◽  
Xiao-Yuan Jia ◽  
You-Min Feng
Keyword(s):  
Biological Activity ◽  
Disulfide Bonds ◽  
Negative Charge ◽  
Disulfide Bridge ◽  
Site Directed Mutagenesis ◽  
Side Chain ◽  
Insulin Analogs ◽  
High Biological Activity ◽  
Chemical Groups ◽  
Structure And Activity

Abstract Insulin contains three disulfide bonds, one intrachain bond, A6–A11, and two interchain bonds, A7–B7 and A20–B19. Site-directed mutagenesis results (the two cysteine residues of disulfide A7–B7 were replaced by serine) showed that disulfide A7–B7 is crucial to both the structure and activity of insulin. However, chemical modification results showed that the insulin analogs still retained relatively high biological activity when A7Cys and B7Cys were modified by chemical groups with a negative charge. Did the negative charge of the modification groups restore the loss of activity and/or the disturbance of structure of these insulin analogs caused by deletion of disulfide A7–B7? To answer this question, an insulin analog with both A7Cys and B7Cys replaced by Glu, which has a long side-chain and a negative charge, was prepared by protein engineering, and its structure and activity were analyzed. Both the structure and activity of the present analog are very similar to that of the mutant with disulfide A7–B7 replaced by Ser, but significantly different from that of wild-type insulin. The present results suggest that removal of disulfide A7–B7 will result in serious loss of biological activity and the native conformation of insulin, even if the disulfide is replaced by residues with a negative charge.

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

scholarly journals Arsenoplatin-Ferritin Nanocage: Structure and Cytotoxicity

2021 ◽  
Vol 22 (4) ◽  
pp. 1874
Author(s):  
Giarita Ferraro ◽  
Alessandro Pratesi ◽  
Damiano Cirri ◽  
Paola Imbimbo ◽  
Daria Maria Monti ◽  
...  
Keyword(s):  
Biological Activity ◽  
Diffraction Data ◽  
Inductively Coupled Plasma ◽  
Emission Spectroscopy ◽  
Atomic Emission ◽  
Side Chain ◽  
Plasma Atomic Emission ◽  
Average Amount ◽  
X Ray ◽  
Inductively Coupled

Arsenoplatin-1 (AP-1), the prototype of a novel class of metallodrugs containing a PtAs(OH)2 core, was encapsulated within the apoferritin (AFt) nanocage. UV-Vis absorption spectroscopy and inductively coupled plasma-atomic emission spectroscopy measurements confirmed metallodrug encapsulation and allowed us to determine the average amount of AP-1 trapped inside the cage. The X-ray structure of AP-1-encapsulated AFt was solved at 1.50 Å. Diffraction data revealed that an AP-1 fragment coordinates the side chain of a His residue. The biological activity of AP-1-loaded AFt was comparatively tested on a few representative cancer and non-cancer cell lines. Even though the presence of the cage reduces the overall cytotoxicity of AP-1, it improves its selectivity towards cancer cells.

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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