Very thermostable energetic materials based on a fused-triazole: 3,6-diamino-1H-[1,2,4]triazolo[4,3-b][1,2,4]triazole

2021 ◽  
Vol 45 (1) ◽  
pp. 85-91
Author(s):  
Yongxing Tang ◽  
Ziwei An ◽  
Ajay Kumar Chinnam ◽  
Richard J. Staples ◽  
Jean'ne M. Shreeve

The fused-triazole backbone 1H-[1,2,4]triazolo[4,3-b][1,2,4]triazole with two C-amino groups gave a highly thermally energetic compound.

2017 ◽  
Vol 95 (5) ◽  
pp. 505-511 ◽  
Author(s):  
Qiong Wu ◽  
Linghua Tan ◽  
Zusheng Hang ◽  
Weihua Zhu

A new powerful zero-hydrogen energetic compound DNDOBTT (2,7-dinitro-4N,9N-dioxide-bis[1,2,4]-triazolo)[1,5-b:1′,5′e][1,2,4,5] tetrazine) was produced by a new design concept of achieving a balance among the parent compound, nitro groups, and N-oxides. Its structure and properties was studied by the density functional theory. The breaking of N–N bond in the tetrazine ring is an initial decomposition step of DNDOBTT, and the energy barrier was predicted to be 175 kJ·mol−1. DNDOBTT has comparable detonation performance with some CHNO energetic compounds, including the most powerful ONC (octanitrocubane), whereas its sensitivity and thermal stability are obviously lower and better than those of ONC, respectively, indicating that DNDOBTT has both the high energy and reduced sensitivity and may be a valuable candidate for experiments. Therefore, a new novel energetic material DNDOBTT with good overall performance has been obtained successfully by the new design concept, and it may be applied to design and develop other novel improved zero-hydrogen energetic materials.


2016 ◽  
Vol 45 (44) ◽  
pp. 17956-17965 ◽  
Author(s):  
Chuan Li ◽  
Man Zhang ◽  
Qishan Chen ◽  
Yingying Li ◽  
Huiqi Gao ◽  
...  

A new C–N linked heterocoupled energetic compound and its energetic salts have been prepared as heat-resistant energetic materials.


2019 ◽  
Vol 55 (61) ◽  
pp. 8979-8982 ◽  
Author(s):  
Lu Hu ◽  
Ping Yin ◽  
Gregory H. Imler ◽  
Damon A. Parrish ◽  
Haixiang Gao ◽  
...  

Energetic materials with N-oxide and amino groups suggest a promising alternative for the design of high-energy materials with low sensitivity.


2019 ◽  
Vol 43 (41) ◽  
pp. 16300-16304 ◽  
Author(s):  
Wangying Zhu ◽  
Zhiwen Ye ◽  
Zhen Dong

A promising fused energetic compound is investigated through the cooperation between nitramino-1,2,5-oxadiazole and fused high-nitrogen backbone.


Author(s):  
James F. Hainfeld ◽  
Frederic R. Furuya

Glutaraldehyde is a useful tissue and molecular fixing reagents. The aldehyde moiety reacts mainly with primary amino groups to form a Schiff's base, which is reversible but reasonably stable at pH 7; a stable covalent bond may be formed by reduction with, e.g., sodium cyanoborohydride (Fig. 1). The bifunctional glutaraldehyde, (CHO-(CH2)3-CHO), successfully stabilizes protein molecules due to generally plentiful amines on their surface; bovine serum albumin has 60; 59 lysines + 1 α-amino. With some enzymes, catalytic activity after fixing is preserved; with respect to antigens, glutaraldehyde treatment can compromise their recognition by antibodies in some cases. Complicating the chemistry somewhat are the reported side reactions, where glutaraldehyde reacts with other amino acid side chains, cysteine, histidine, and tyrosine. It has also been reported that glutaraldehyde can polymerize in aqueous solution. Newer crosslinkers have been found that are more specific for the amino group, such as the N-hydroxysuccinimide esters, and are commonly preferred for forming conjugates. However, most of these linkers hydrolyze in solution, so that the activity is lost over several hours, whereas the aldehyde group is stable in solution, and may have an advantage of overall efficiency.


1983 ◽  
Vol 49 (03) ◽  
pp. 208-213
Author(s):  
A J Osbahr

SummaryThe modification of canine fibrinogen with citraconic anhydride modified the ε-amino groups of the fibrinogen and at the same time generated additional negative charges into the protein. The addition of thrombin to the modified fibrinogen did not induce polymerization; however, the fibrinopeptide was released at a faster rate than from the unmodified fibrinogen. The physical properties of the citraconylated fibrinogen were markedly altered by the modification of 50-60 lysine residues in one hour. A modified fibrinopeptide-A was released by thrombin from the modified fibrinogen and was electrophoretically more anionic than the unmodified fibrinopeptide-A. Edman analysis confirmed the modification of the lysine residue present in the peptide. The rate of removal of citraconylated fibrinopeptide-A from modified fibrinogen by thrombin was 30 to 40 percent greater than the cleavage of unmodified fibrinopeptide-A from unmodified fibrinogen. However, the modification of 60 or more lysine residues in the fibrinogen produced a decrease in the rate of cleavage of citraconylated fibrinopeptide-A. The results suggest that additional negative charge in the vicinity of the attachment of fibrinopeptide-A to canine fibrinogen aids in the removal of the peptide by thrombin.


1963 ◽  
Vol 42 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Arthur I. Cohen ◽  
Edward H. Frieden

ABSTRACT A number of corticotrophin analogues have been prepared, some of which potentiate the biological activity of the untreated hormone in vitro. The free amino groups of corticotrophin appear to be essential not only for hormonal activity, but also for the interaction of the analogues with the tissue corticotrophin inactivating system which is assumed to account for the potentiating effect.


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