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The scientific research interests of our laboratory are focused in the fields of Structural Biology / Molecular Biophysics and Computational Biology / Bioinformatics. More specifically, we are dealing with:
Structural and self-assembly studies of silkmoth chorion peptide analogues as novel self-assembled polymers with amyloid properties. These studies may lead to the construction of novel biomaterials with extraordinary physical properties. We determined that silkmoth chorion is a natural, protective amyloid and we proposed, for the first time worldwide, the existence of natural, functional amyloids. Currently, we are also experimentally studying the role of a great variety of amyloidogenic (‘aggregation-prone’)-peptides, predicted by our AMYLPRED prediction algorithm, in several widespread and also rare pathological amyloidoses. We are particularly interested to ‘hack’ the amyloid code, if such a code exists.
Development of algorithms that predict the structure, function and interaction of proteins from sequence alone. These algorithms, frequently, have genome-wide applications. The knowledge expertise of our team, in combination with the sophisticated tools that we develop, enables us to build curated, expert, knowledge-based, relational protein and DNA biological databases. Recently, special emphasis is given to the development of methods and software for the prediction of structure, function and interactions of transmembrane proteins and the development of relational/object oriented databases of transmembrane proteins. We have focused on the GPCRs - G-proteins - Effectors system and on the outer membrane proteins (OMPs) of Gram-negative bacteria, which are both of great pharmacological interest. Unique, worldwide, relational databases of GPCRs - G-protein - Effectors interactions and also a database of OMPs, developed by our team, are freely accessible through the Internet.
Structural and self-assembly studies of fibrous proteins, which form extracellular, proteinaceous structures of physiological importance like lepidopteran, dipteran and fish chorions. Model structures of silkmoth chorion proteins and their interactions have been proposed. Also, we are studying chitin-protein interactions for the formation of arthropod cuticle. We have recently proposed a model structure of cuticular proteins and we developed a universal, freely available through the Internet, cuticular protein relational databas
Studies of water soluble, globular protein structure, function and interactions with small molecules, aiming at the determination of the mechanisms of molecular recognition at/or near atomic resolution. Model systems of study include: a) the interactions of the lectin concanavalin A (conA) with saccharides and hydrophobic molecules, b) the enzyme DHFR and its interactions with inhibitors, which act as antibacterial and anticancer agents.
Structural and self-assembly studies of silkmoth chorion peptide analogues as novel self-assembled polymers with amyloid properties. These studies may lead to the construction of novel biomaterials with extraordinary physical properties. We determined that silkmoth chorion is a natural, protective amyloid and we proposed, for the first time worldwide, the existence of natural, functional amyloids. Currently, we are also experimentally studying the role of a great variety of amyloidogenic (‘aggregation-prone’)-peptides, predicted by our AMYLPRED prediction algorithm, in several widespread and also rare pathological amyloidoses. We are particularly interested to ‘hack’ the amyloid code, if such a code exists.
Development of algorithms that predict the structure, function and interaction of proteins from sequence alone. These algorithms, frequently, have genome-wide applications. The knowledge expertise of our team, in combination with the sophisticated tools that we develop, enables us to build curated, expert, knowledge-based, relational protein and DNA biological databases. Recently, special emphasis is given to the development of methods and software for the prediction of structure, function and interactions of transmembrane proteins and the development of relational/object oriented databases of transmembrane proteins. We have focused on the GPCRs - G-proteins - Effectors system and on the outer membrane proteins (OMPs) of Gram-negative bacteria, which are both of great pharmacological interest. Unique, worldwide, relational databases of GPCRs - G-protein - Effectors interactions and also a database of OMPs, developed by our team, are freely accessible through the Internet.
Structural and self-assembly studies of fibrous proteins, which form extracellular, proteinaceous structures of physiological importance like lepidopteran, dipteran and fish chorions. Model structures of silkmoth chorion proteins and their interactions have been proposed. Also, we are studying chitin-protein interactions for the formation of arthropod cuticle. We have recently proposed a model structure of cuticular proteins and we developed a universal, freely available through the Internet, cuticular protein relational databas
Studies of water soluble, globular protein structure, function and interactions with small molecules, aiming at the determination of the mechanisms of molecular recognition at/or near atomic resolution. Model systems of study include: a) the interactions of the lectin concanavalin A (conA) with saccharides and hydrophobic molecules, b) the enzyme DHFR and its interactions with inhibitors, which act as antibacterial and anticancer agents.
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Frontiers Bioinform. (2021): 646581
Katerina C Nastou, Eleftheria G Karataraki,Nikos C Papandreou,Anna-Isavella G Rerra, Vassiliki P Grimanelli,Ilias Maglogiannis,Stavros J Hamodrakas,Vassiliki A Iconomidou
International Conference of Computational Methods in Sciences and Engineering 2004 (ICCMSE 2004)pp.53-56, (2019)
Konstantina V Biza,Katerina C Nastou,Paraskevi L Tsiolaki, Chara V Mastrokalou,Stavros J Hamodrakas,Vassiliki A Iconomidou
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