scholarly journals ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships

2018 ◽  
Vol 20 (1) ◽  
pp. 30 ◽  
Author(s):  
Benildo Cavada ◽  
Vanir Pinto-Junior ◽  
Vinicius Osterne ◽  
Kyria Nascimento
Keyword(s):  
Biological Activity ◽  
Structural Properties ◽  
Concanavalin A ◽  
Biological Activities ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Carbohydrate Specificity ◽  
High Similarity ◽  
Antitumor Activities ◽  
Reversible Binding

Lectins are a widely studied group of proteins capable of specific and reversible binding to carbohydrates. Undoubtedly, the best characterized are those extracted from plants of the Leguminosae family. Inside this group of proteins, those from the Diocleinae subtribe have attracted attention, in particular Concanavalin A (ConA), the best-studied lectin of the group. Diocleinae lectins, also called ConA-like lectins, present a high similarity of sequence and three-dimensional structure and are known to present inflammatory, vasoactive, antibiotic, immunomodulatory and antitumor activities, among others. This high similarity of lectins inside the ConA-like group makes it possible to use them to study structure/biological activity relationships by the variability of both carbohydrate specificity and biological activities results. It is in this context the following review aims to summarize the most recent data on the biochemical and structural properties, as well as biological activities, of ConA-like lectins and the use of these lectins as models to study structure/biological activity relationships.

Viscoelastic and Structural Properties of a Phenyl-Modified Polysiloxane System with a Three-Dimensional Structure

2006 ◽  
Vol 110 (14) ◽  
pp. 7321-7327 ◽  
Author(s):  
Hiroshi Kakiuchida ◽  
Masahide Takahashi ◽  
Yomei Tokuda ◽  
Hirokazu Masai ◽  
Minoru Kuniyoshi ◽  
...  
Keyword(s):  
Structural Properties ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

ConBr, the Lectin from Canavalia brasiliensis Mart. Seeds: Forty Years of Research

2019 ◽  
Vol 20 (6) ◽  
pp. 600-613 ◽  
Author(s):  
Benildo Sousa Cavada ◽  
Vinicius Jose Silva Osterne ◽  
Vanir Reis Pinto-Junior ◽  
Kyria Santiago Nascimento
Keyword(s):  
Physicochemical Properties ◽  
Concanavalin A ◽  
Biological Activities ◽  
Biotechnological Applications ◽  
Reversible Binding ◽  
Isolation And Characterization ◽  
Look Ahead ◽  
The Subject ◽  
Canavalia Brasiliensis

Lectins are defined as proteins or glycoproteins capable of specific and reversible binding to carbohydrates. Inside this group of proteins, the most well-studied lectins belong to the Leguminosae family, and inside this family, the Diocleinae subtribe includes the most characterized lectin Concanavalin A (ConA), as well as ConBr, the lectin from Canavalia brasiliensis, the subject of this review. Since 1979, several studies have been published in the literature regarding this lectin, from its isolation and characterization to its several biological activities. This year, 2019, will mark 40 years since researchers have begun to study ConBr and 100 years since the discovery of ConA, making 2019 a momentous year for lectinology. Owing to the abundance of studies involving ConBr, this review will focus on ConBr’s purification, physicochemical properties, functional and structural analyses, biological activities and biotechnological applications. This will give researchers a broad glimpse into the potential of this lectin, as well as it characteristics, as we look ahead to its expanding applications in glycomics and biotechnology.

scholarly journals IN SILICO STUDIES OF SOPHORAFLAVANONE G: QUANTUM CHARACTERIZATION AND ADMET

2020 ◽  
Vol 7 (11) ◽  
pp. 160-179 ◽  
Author(s):  
David Lopes Santiago De Oliveira ◽  
Emanuelle Machado Marinho ◽  
Francisco Nithael Melo Lucio ◽  
Marcia Machado Marinho ◽  
Francisco Rogênio Da Silva Mendes ◽  
...  
Keyword(s):  
Estrogen Receptor Alpha ◽  
Therapeutic Potential ◽  
Early Stage ◽  
Biological Activities ◽  
Three Dimensional ◽  
New Drugs ◽  
Dimensional Structure ◽  
Skin Permeability ◽  
Biological Targets ◽  
In Silico Studies

Currently, the search for new drugs with greater therapeutic potential and less side effects has been fostered by the advancement of the use of molecular modeling drugs, which in addition to supporting the full characterization of the molecule, allow simple algorithms to predict pharmacokinetic. In this context the present work aimed to perform the electronic / structural characterization, to evaluate the pharmacokinetic properties and to perform a virtual screening of the possible biological targets of Sophoraflavonone G, a promising flavonone, which presents several pharmacological properties. Sophoraflavanone G was geometrically optimized by semi-empirical quantum calculations, plot the MESP, identifying the nucleophilic sites. Using the boundary orbitals, it was possible to identify a greater tendency for electron donation in relation to Naringeni, with lower ionization potential, higher hardness and less softness. With respect to pharmacokinetics Sophoraflavonone G confirmed the safety of the compound for oral administration with good skin permeability, which allows applications in topical formulations. Presents indications for gastro intestinal absorption, as for possible interactions with biological targets, interaction with the estrogen receptor alpha, sodium / glucose co-transporter 2, beta-secretase 1, cyclooxygenase-1.The data obtained from an early stage for a comparative analysis between its analogues and fundamental for future studies of relationships between the three-dimensional structure of Sophoraflavanone G and its biological activities.

scholarly journals The Covalent and Three-Dimensional Structure of Concanavalin A

1972 ◽  
Vol 69 (9) ◽  
pp. 2580-2584 ◽  
Author(s):  
G. M. Edelman ◽  
B. A. Cunningham ◽  
G. N. Reeke ◽  
J. W. Becker ◽  
M. J. Waxdal ◽  
...  
Keyword(s):  
Concanavalin A ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure
Sign in / Sign up

Export Citation Format

Share Document