SYNTHÈSES DE COURTS PEPTIDES RENFERMANT DES ACIDES AMINO-1 CYCLOALKYL CARBOXYLIQUES

1961 ◽  
Vol 39 (6) ◽  
pp. 1309-1320 ◽  
Author(s):  
Patrice Tailleur ◽  
Louis Berlinguet
Keyword(s):  
Amino Acids ◽  
Carboxylic Acids ◽  
Small Peptides ◽  
Subsequent Hydrolysis ◽  
Methods Of Synthesis ◽  
Natural Amino Acids ◽  
Hydrolysis Of

Using classical methods of synthesis nine small peptides containing amino-1 cycloalkyl carboxylic acids have been synthesized. The cyclic acids have been placed either at the N-terminal or at the C-terminal positions or in between two natural amino acids, glycine and DL-phenylalanine.The cyclization of two dipeptides into a substituted diketopiperazine, and the subsequent hydrolysis of this compound have been studied.

Review on Clinical Application of Deproteinized Calf Blood Extractive

2014 ◽  
Vol 675-677 ◽  
pp. 1617-1621
Author(s):  
Guang Yu Xu ◽  
Li Na Chen ◽  
Zhuo Yuan Xin ◽  
Yu Xin Liu ◽  
Tan Cheng Li ◽  
...  
Keyword(s):  
Amino Acids ◽  
Clinical Application ◽  
Adenosine Triphosphate ◽  
Tissue Repair ◽  
Calf Serum ◽  
Bioactive Components ◽  
Small Peptides ◽  
Pharmacological Activities ◽  
Tissue Repair And Regeneration ◽  
Natural Amino Acids

Deproteinized calf blood extractive was bioactive components, including natural amino acids, small peptides, glycolipids, nucleosides and carbohydrates, extracted from calf serum. The main pharmacological activities of deproteinized calf blood extractives contained several vital processes, such as enhancing the uptake and utilization of oxygen and glucose, boosting the synthesis of adenosine triphosphate, promoting the transport of nutrients, facilitating the tissue repair and regeneration. In this article, from the review of the researches on the clinical application of deproteinized calf blood extractives, we concluded that it was worth on clinical promotion.

scholarly journals The Aminopropylation of Bovine Serum Albumin

1967 ◽  
Vol 20 (1) ◽  
pp. 233 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Amino Acids ◽  
Alkylating Agents ◽  
Side Reactions ◽  
Contrast Reaction ◽  
Ph Values ◽  
Subsequent Hydrolysis ◽  
Positive Peak ◽  
State Of Affairs ◽  
Hydrolysis Of ◽  
Quantitative Recovery

After the reaction of reduced BSAt with BPA at pH 10�6 and subsequent hydrolysis of the protein with 6N HCl, only 40% of the lysine present in the unmodified protein can be accounted for on chromatographic analysis of the hydrolysate; a similar loss is observed of the SAPC into which the original cystine, which has totally disappeared, is presumably initially all converted. In place of these amino acids, a "neutral" ninhydrin-positive peak is observed which accounts approximately quantitatively for the missing lysine. The reaction at pH 8� 6 with IP A leads to a quantitative recovery of SAPC with no loss of lysine. In contrast, reaction for the same times at both pH values with BEA leads to quantitative recovery of all amino acids including SAEC. Although the reaction ofIP A with thiols at pH 8�6 is very slow compared with that of other alkylating agents, the relative absence of side reactions may be compared with the state of affairs when methyl iodide is used for an equivalent period in the same relative quantities, when there is extensive alteration of lysine, histidine, methionine, and S-methylcysteine.

S1′ and S2′ subsite specificities of human plasma kallikrein and tissue kallikrein 1 for the hydrolysis of peptides derived from the bradykinin domain of human kininogen

2008 ◽  
Vol 389 (12) ◽  
Author(s):  
Aurelio Resende Lima ◽  
Fabiana M. Alves ◽  
Pedro Francisco Ângelo ◽  
Douglas Andrade ◽  
Sachiko I. Blaber ◽  
...  
Keyword(s):  
Amino Acids ◽  
Human Plasma ◽  
Receptor Agonist ◽  
Plasma Kallikrein ◽  
Tissue Kallikrein ◽  
Charged Amino Acids ◽  
B1 Receptor ◽  
Lower Specificity ◽  
Natural Amino Acids ◽  
Hydrolysis Of

AbstractThe S1′ and S2′ subsite specificities of human tissue kallikrein 1 (KLK1) and human plasma kallikrein (HPK) were examined with the peptide series Abz-GFSPFRXSRIQ-EDDnp and Abz-GFSPFRSXRIQ-EDDnp [X=natural amino acids or S(PO3H2)]. KLK1 efficiently hydrolyzed most of the peptides except those containing negatively charged amino acids at P1′ and P2′ positions. Abz-GFSPFRSSRIQ-EDDnp, as in human kininogen, is the best substrate for KLK1 and exclusively cleaved the R-S bond. All other peptides were cleaved also at the F-R bond. The synthetic human kininogen segment Abz-MISLMKRPPGFSPFRS390S391RI-NH2was hydrolyzed by KLK1 first at R-S and then at M-K bonds, releasing Lys-bradykinin. In the S390and S391phosphorylated analogs, this order of hydrolysis was inverted due to the higher resistance of the R-S bond. Abz-MISLMKRPPG-FSPFRSS(PO3H2)391RI-NH2was hydrolyzed by KLK1 at M-K and mainly at the F-R bond, releasing des-(Arg9)-Lys-Bk which is a B1 receptor agonist. HPK cleaved all the peptides at R and showed restricted specificity for S in the S1′ subsite, with lower specificity for the S2′ subsite. Abz-MISLMKRPPGFSPFRSSRI-NH2was efficiently hydrolyzed by HPK under bradykinin release, while the analogs containing S(PO3H2) were poorly hydrolyzed. In conclusion, S1′ and S2′ subsite specificities of KLK1 and HPK showed peculiarities that were observed with substrates containing the amino acid sequence of human kininogen.

Chiral amino alcohols derived from natural amino acids as chiral solvating agents for carboxylic acids

2008 ◽  
Vol 19 (10) ◽  
pp. 1193-1199 ◽  
Author(s):  
Wenge Wang ◽  
Xiumin Shen ◽  
Fengnian Ma ◽  
Zijing Li ◽  
Cong Zhang
Keyword(s):  
Amino Acids ◽  
Carboxylic Acids ◽  
Amino Alcohols ◽  
Natural Amino Acids ◽  
Chiral Amino Alcohols

scholarly journals Steric and Electronic Effects in the Synthesis and Regioselective Hydrolysis of Unsymmetrical Imides

2015 ◽  
Vol 68 (12) ◽  
pp. 1854 ◽  
Author(s):  
Jing Shang ◽  
Aysa Pourvali ◽  
James R. Cochrane ◽  
Craig A. Hutton
Keyword(s):  
Carboxylic Acid ◽  
Carboxylic Acids ◽  
Trifluoroacetic Acid ◽  
Coupling Reaction ◽  
Pivalic Acid ◽  
Electronic Effects ◽  
Subsequent Hydrolysis ◽  
Reaction Proceeds ◽  
Hydrolysis Of ◽  
Regioselective Hydrolysis

The AgI-promoted coupling reaction of thioamides and carboxylic acids is shown to be a useful method for the generation of unsymmetrical imides. The reaction proceeds efficiently with unhindered and electron-rich or neutral coupling partners, but not with hindered thioamides (such as thiopivalamides) or electron deficient thioamides (such as trifluorothioacetamides). Intriguingly, thioformamides are also ineffective coupling partners, despite having minimal steric or electronic influence. Hindered carboxylic acid coupling partners (such as pivalic acid) are tolerated, but electron deficient acids, such as trifluoroacetic acid, are ineffective coupling partners. Furthermore, an interplay of both steric and electronic effects is observed in the subsequent hydrolysis of unsymmetrical imides. Imides with a dimethoxybenzoyl group give high regioselectivity upon hydrolysis, favouring cleavage of the distal acyl group. Imides with a p-nitrobenzoyl or pivaloyl group give reversed selectivity, favouring cleavage of the proximal acyl group.

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