Shortened Insulin Analogues:  Marked Changes in Biological Activity Resulting from Replacement of TyrB26 and N-Methylation of Peptide Bonds in the C-Terminus of the B-Chain†

Biochemistry ◽  
2004 ◽  
Vol 43 (8) ◽  
pp. 2323-2331 ◽  
Author(s):  
Lenka Žáková ◽  
Tomislav Barth ◽  
Jiří Jiráček ◽  
Jana Barthová ◽  
Štefan Zórad
Keyword(s):  
Biological Activity ◽  
Insulin Analogues ◽  
Peptide Bonds ◽  
C Terminus

Synthesis and Biological Activity of Four Vasopressin Analogs Modified in Position 3 with β-Thienylalanine

1995 ◽  
Vol 60 (4) ◽  
pp. 681-686 ◽  
Author(s):  
Jiřina Slaninová ◽  
Malgorzata Czaja ◽  
Bernard Lammek
Keyword(s):  
Biological Activity ◽  
Arginine Vasopressin ◽  
Peptide Bonds

Four new analogs of arginine-vasopressin substituted in position 3 with β-thienylalanine were synthesized on chloromethylated resin using Boc strategy and DCC or DCC-HOBt to form peptide bonds. The activity of the agonists is not much different in comparison to the unsubstituted compounds. However, the potency of one of the antagonists is strongly reduced.

scholarly journals Thermal Synthesis of Polypeptides from N-Butyloxycarbonyl Oligopeptides Containing Aspartyl Residue at C-Terminus

2017 ◽  
Vol 2017 ◽  
pp. 1-16
Author(s):  
Toratane Munegumi ◽  
Takafumi Yamada
Keyword(s):  
Aspartic Acid ◽  
Organic Synthesis ◽  
Prebiotic Chemistry ◽  
Average Molecular Weight ◽  
Carboxyl Terminus ◽  
Peptide Bonds ◽  
Thermal Synthesis ◽  
Thermal Reactions ◽  
C Terminus ◽  
Aspartyl Residue

The thermal reactions of amino acids have been investigated for pure organic synthesis, materials preparation in industry, and prebiotic chemistry. N-t-Butyloxycarbonyl aspartic acid (Boc-Asp) releases 2-butene and carbon dioxide upon heating without solvents. The resulting mixture of the free molten aspartic acid was dehydrated to give peptide bonds. This study describes the thermal reactions of N-t-butyloxycarbonyl peptides (Boc-Gly-L-Asp, Boc-L-Ala-L-Asp, Boc-L-Val-L-Asp, and Boc-Gly-Gly-L-Asp) having an aspartic residue at the carboxyl terminus. The peptides were deprotected upon heating at a constant temperature between 110 and 170°C for 1 to 24 h to afford polypeptides in which the average molecular weight reached 7800.

Effect of N-methylation of selected peptide bonds on the biological activity of insulin. [2-N-Methylisoleucine-A]insulin

2009 ◽  
Vol 30 (4) ◽  
pp. 460-473 ◽  
Author(s):  
HIROSHI OGAWA ◽  
G. THOMPSON BURKE ◽  
JACOB D. CHANLEY ◽  
PANAYOTIS G. KATSOYANNIS
Keyword(s):  
Biological Activity ◽  
Peptide Bonds

Attachment of C-Terminus of SDF-1 Enhances the Biological Activity of Its N-Terminal Peptide

1999 ◽  
Vol 264 (1) ◽  
pp. 42-47 ◽  
Author(s):  
Jiansong Luo ◽  
Zhaowen Luo ◽  
Naiming Zhou ◽  
James W Hall ◽  
Ziwei Huang
Keyword(s):  
Biological Activity ◽  
C Terminus

Insulin Analogues with Modifications at Position B26. Divergence of Binding Affinity and Biological Activity†

Biochemistry ◽  
2008 ◽  
Vol 47 (21) ◽  
pp. 5858-5868 ◽  
Author(s):  
Lenka Žáková ◽  
Ludmila Kazdová ◽  
Ivona Hančlová ◽  
Eva Protivínská ◽  
Miloslav Šanda ◽  
...  
Keyword(s):  
Biological Activity ◽  
Binding Affinity ◽  
Insulin Analogues

Equivalent In Vivo Biological Activity of Insulin Analogues and Human Insulin Despite Different In Vitro Potencies

Diabetes ◽  
1990 ◽  
Vol 39 (9) ◽  
pp. 1033-1039 ◽  
Author(s):  
U. Ribel ◽  
P. Hougaard ◽  
K. Drejer ◽  
A. R. Sorensen
Keyword(s):  
Biological Activity ◽  
Human Insulin ◽  
Insulin Analogues

scholarly journals A bipartite nuclear localization signal in the retinoblastoma gene product and its importance for biological activity.

1993 ◽  
Vol 13 (8) ◽  
pp. 4588-4599 ◽  
Author(s):  
E Zacksenhaus ◽  
R Bremner ◽  
R A Phillips ◽  
B L Gallie
Keyword(s):  
Biological Activity ◽  
Transcription Factors ◽  
Gene Product ◽  
Nuclear Localization ◽  
Simian Virus 40 ◽  
T Antigen ◽  
Retinoblastoma Gene ◽  
C Terminus ◽  
Retinoblastoma Gene Product ◽  
Cellular Transcription

The retinoblastoma gene product, p110RB1, appears to regulate cell growth by modulating the activities of nuclear transcription factors. The elements that specify the transport of p110RB1 into the nucleus have not yet been explored. We now report the identification of a basic region, KRSAEGGNPPKPLKKLR, in the C terminus of p110RB1, which has sequence similarity to known bipartite nuclear localization signals (NLSs). A two-amino-acid mutation introduced into this putative NLS [to give mutant NLS(NQ)] or deletion of the entire NLS (delta NLS) abrogated exclusive nuclear localization, yielding proteins which were distributed either equally throughout the cell or predominantly in the cytoplasm. A mutant protein [NLS(NQ)/delta 22] containing both the mutated NLS and a deletion of exon 22, previously shown to disrupt the interaction of p110RB1 with several cellular transcription factors and oncoproteins, accumulated only in the cytoplasm. When fused to the C terminus of Escherichia coli beta-galactosidase, the RB1 NLS directed this protein to the nucleus, indicating that the motif is not only necessary but also sufficient for nuclear transport. Neither NLS(NQ) nor delta NLS was hyperphosphorylated in vivo, but both retained their abilities to interact, in vitro, with simian virus 40 large T antigen, adenovirus E1a, and the cellular transcription factor E2F. When transfected at multiple copy number, the NLS mutant alleles displayed reduced biological activity, measured by inhibition of growth of the osteogenic sarcoma cell line Saos-2, which has no wild-type RB1. Naturally occurring mutations and deletions in exon 25 of RB1 which disrupt the NLS may lead to partial or complete inactivation of p110RB1 and may be responsible for some retinoblastoma and other tumors.

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