The Self-Recognition and Self-Assembly of Folic Acid Salts in Isotropic Water Solution

1996 ◽  
Vol 79 (1) ◽  
pp. 220-234 ◽  
Author(s):  
Giovanni Gottarelli ◽  
Elisabetta Mezzina ◽  
Gian Piero Spada ◽  
Flavio Carsughi ◽  
Giovanni Di Nicola ◽  
...  
1994 ◽  
Vol 116 (16) ◽  
pp. 7064-7071 ◽  
Author(s):  
Federica Ciuchi ◽  
Giovanni Di Nicola ◽  
Hermann Franz ◽  
Giovanni Gottarelli ◽  
Paolo Mariani ◽  
...  

Author(s):  
Giovanni Gottarelli ◽  
Gian Piero Spada ◽  
Paolo Mariani
Keyword(s):  

Langmuir ◽  
2020 ◽  
Vol 36 (35) ◽  
pp. 10519-10527
Author(s):  
Jiahui Chen ◽  
Kun Qian ◽  
Kexing Xiao ◽  
Jiancheng Luo ◽  
Hui Li ◽  
...  

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1084 ◽  
Author(s):  
Shaoming Jin ◽  
Zhongyao Du ◽  
Pengjie Wang ◽  
Huiyuan Guo ◽  
Hao Zhang ◽  
...  

Folic acid has been widely introduced into nano-drug delivery systems to give nanoparticle-targeted characteristics. However, the poor water solubility of folic acid may hinder the exploitation of its ability to load antineoplastic drugs. In the present study, we designed a new folate derivative (FA-2-DG) synthesized from folic acid and 2-Deoxyglucose (2-DG). The aim of this study was to evaluate the self-assembly characteristics of FA-2-DG, and its ability of loading cisplatin. The critical micelle concentration was 7.94 × 10−6 mol L−1. Fourier transform infrared spectroscopy indicated that hydrogen bonding interaction is a main driving force for the self–assembly of FA-2-DG. The particle was stable in pure water or 0.5% bovine serum albumin dispersions. By forming a coordination bond, the particles assembled from FA-2-DG can load cisplatin. The loading efficiency was maximal when the molar ratio of FA-2-DG to cisplatin was 2:1.


1993 ◽  
Vol 32 (2) ◽  
pp. 248-250 ◽  
Author(s):  
Stefania Bonazzi ◽  
Monica Miranda DeMorais ◽  
Giovanni Gottarelli ◽  
Paolo Mariani ◽  
Gian Piero Spada

RSC Advances ◽  
2014 ◽  
Vol 4 (69) ◽  
pp. 36633-36639 ◽  
Author(s):  
Pengyao Xing ◽  
Xiaoxiao Chu ◽  
Mingfang Ma ◽  
Shangyang Li ◽  
Yimeng Zhang ◽  
...  

Utilizing the self-assembly of folic acid/melamine complexes in water, we realized the construction of spherulites and networks with porous structure from membrane growth and folding.


Author(s):  
M. Kessel ◽  
R. MacColl

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.


Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


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