Structure and activity of corticotrophic peptides: Synthesis and biological activity of two corticotrophic peptides with neutral amino acids in positions 17 and 18

1970 ◽  
Vol 26 (10) ◽  
pp. 1050-1052 ◽  
Author(s):  
M. Brugger ◽  
P. Barthe ◽  
P. A. Desaulles
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Neutral Amino Acids ◽  
Peptides Synthesis ◽  
Structure And Activity

N-Methylated α-Amino Acids And Peptides: Synthesis And Biological Activity

2016 ◽  
Vol 16 (9) ◽  
pp. 683-690 ◽  
Author(s):  
Maria Luisa Di Gioia ◽  
Antonella Leggio ◽  
Francesca Malagrinò ◽  
Emanuela Romio ◽  
Carlo Siciliano ◽  
...  
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Peptides Synthesis

β2-Amino Acids with Proteinogenic Side Chains and Corresponding Peptides: Synthesis, Secondary Structure, and Biological Activity

ChemInform ◽  
2006 ◽  
Vol 37 (31) ◽  
Author(s):  
Marino A. Campo ◽  
Jaime Escalante ◽  
Radovan Sebesta
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Secondary Structure ◽  
Side Chains ◽  
Peptides Synthesis

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.

ChemInform Abstract: INVERSE SUBSTRATES. IX. AMIDINOPHENYL ESTERS DERIVED FROM AMINO ACIDS AND PEPTIDES: SYNTHESIS AND PROPERTIES AS TRYPSIN SUBSTRATES

1980 ◽  
Vol 11 (45) ◽  
Author(s):  
T. FUJIOKA ◽  
K. TANIZAWA ◽  
H. NAKAYAMA ◽  
Y. KANAOKA
Keyword(s):  
Amino Acids ◽  
Peptides Synthesis

Atypical amino acids inhibit histidine, valine, or lysine transport into rat brain

1983 ◽  
Vol 245 (4) ◽  
pp. R556-R563 ◽  
Author(s):  
J. K. Tews ◽  
A. E. Harper
Keyword(s):  
Amino Acids ◽  
Rat Brain ◽  
Blood Brain Barrier ◽  
Brain Slices ◽  
Aromatic Amino Acids ◽  
Brain Barrier ◽  
Basic Amino Acids ◽  
Large Neutral Amino Acids ◽  
Neutral Amino Acids ◽  
Single Meal

Transport of histidine, valine, or lysine into rat brain slices and across the blood-brain barrier (BBB) was determined in the presence of atypical nonprotein amino acids. Competitors of histidine and valine transport in slices were large neutral amino acids including norleucine, norvaline, alpha-aminooctanoate, beta-methylphenylalanine, and alpha-aminophenylacetate. Less effective were aromatic amino acids with ring substituents; ineffective were basic amino acids and omega-amino isomers of norleucine and aminooctanoate. Lysine transport was moderately depressed by homoarginine or ornithine plus arginine; large neutral amino acids were also similarly inhibitory. Histidine or valine transport across the BBB was also strongly inhibited by large neutral amino acids that were the most effective competitors in the slices (norvaline, norleucine, alpha-aminooctanoate, and alpha-aminophenylacetate); homoarginine and 8-aminooctanoate were ineffective. Homoarginine, ornithine, and arginine almost completely blocked lysine transport, but the large neutral amino acids were barely inhibitory. When rats were fed a single meal containing individual atypical large neutral amino acids or homoarginine, brain pools of certain large neutral amino acids or of arginine and lysine, respectively, were depleted.

scholarly journals Characteristics of system ASC for transport of neutral amino acids in the isolated rat hepatocyte.

1981 ◽  
Vol 256 (7) ◽  
pp. 3304-3312
Author(s):  
M.S. Kilberg ◽  
M.E. Handlogten ◽  
H.N. Christensen
Keyword(s):  
Amino Acids ◽  
Rat Hepatocyte ◽  
Neutral Amino Acids ◽  
Isolated Rat

scholarly journals Characteristics of a lysosomal membrane transport system for tyrosine and other neutral amino acids in rat thyroid cells.

1986 ◽  
Vol 261 (36) ◽  
pp. 17107-17112
Author(s):  
J Bernar ◽  
F Tietze ◽  
L D Kohn ◽  
I Bernardini ◽  
G S Harper ◽  
...  
Keyword(s):  
Amino Acids ◽  
Membrane Transport ◽  
Transport System ◽  
Lysosomal Membrane ◽  
Thyroid Cells ◽  
Neutral Amino Acids ◽  
Rat Thyroid

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.

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