Chiral Amplification in Macromolecular Helicity Assisted by Noncovalent Interaction with Achiral Amines and Memory of the Helical Chirality

2004 ◽  
Vol 10 (19) ◽  
pp. 4703-4707 ◽  
Author(s):  
Kazuhide Morino ◽  
Nobuyuki Watase ◽  
Katsuhiro Maeda ◽  
Eiji Yashima
Keyword(s):  
Noncovalent Interaction ◽  
Chiral Amplification ◽  
Helical Chirality

Asymmetric Induction and Amplification in Stereodynamic Catalytic Systems by Noncovalent Interactions

Synlett ◽  
2020 ◽  
Author(s):  
Oliver Trapp ◽  
Jan Felix Scholtes
Keyword(s):  
Noncovalent Interactions ◽  
Noncovalent Interaction ◽  
Kinetic Properties ◽  
Catalytic Systems ◽  
Asymmetric Transformations ◽  
Chemical Systems ◽  
Chiral Induction ◽  
Chiral Amplification ◽  
Biochemical Systems ◽  
Local Transmission

AbstractThe local transmission of chiral information by noncovalent interactions is one of the most fundamental processes broadly found in nature, i.e. in complex biochemical systems. This review summarizes our accomplishments in investigating chiral induction in stereodynamic ligands and catalysts by weak intermolecular interactions. It includes our efforts to characterize numerous stereodynamic compounds in detail with respect to their thermodynamic and kinetic properties. Furthermore, many stereolabile ligands for enantioselective catalysis are described, where directed stereoinduction afforded highly enantio- or diastereoenriched catalysts for subsequent selective asymmetric transformations. Various approaches for the dynamic enrichment of one of the catalyst’s conformers are presented, such as noncovalent interaction of the ligand with a chiral environment or a chiral solute. Finally, successful chemical systems are presented in which a process of chiral induction can be coupled with an autoinductive mechanism triggered by the chirality of its own reaction product, realizing Nature-inspired feedback loops resulting in self-amplifying, enantioselective catalytic reactions.1 Introduction2 Mapping the Stereodynamic Landscape3 Chiral Induction by Noncovalent Interactions4 Autoinduction and Chiral Amplification5 Self-Alignment and Emergence of Chirality6 Conclusion

Molecular Docking and QSAR Studies: Noncovalent Interaction between Acephate Analogous and the Receptor Site of Human Acetylcholinesterase

2013 ◽  
Vol 61 (28) ◽  
pp. 6776-6785 ◽  
Author(s):  
Khodayar Gholivand ◽  
Ali Asghar Ebrahimi Valmoozi ◽  
Hamid R. Mahzouni ◽  
Saied Ghadimi ◽  
Rayhaneh Rahimi
Keyword(s):  
Molecular Docking ◽  
Receptor Site ◽  
Noncovalent Interaction ◽  
Qsar Studies

scholarly journals Vaccinia Virus A26 and A27 Proteins Form a Stable Complex Tethered to Mature Virions by Association with the A17 Transmembrane Protein

2008 ◽  
Vol 82 (24) ◽  
pp. 12384-12391 ◽  
Author(s):  
Amanda R. Howard ◽  
Tatiana G. Senkevich ◽  
Bernard Moss
Keyword(s):  
Vaccinia Virus ◽  
Matrix Protein ◽  
Transmembrane Domain ◽  
Noncovalent Complex ◽  
Transmembrane Protein ◽  
Amino Acid Identity ◽  
Noncovalent Interaction ◽  
Terminal Segment ◽  
Stable Complex ◽  
Cowpox Virus

ABSTRACT During vaccinia virus replication, mature virions (MVs) are wrapped with cellular membranes, transported to the periphery, and exported as extracellular virions (EVs) that mediate spread. The A26 protein is unusual in that it is present in MVs but not EVs. This distribution led to a proposal that A26 negatively regulates wrapping. A26 also has roles in the attachment of MVs to the cell surface and incorporation of MVs into proteinaceous A-type inclusions in some orthopoxvirus species. However, A26 lacks a transmembrane domain, and nothing is known regarding how it associates with the MV, regulates incorporation of the MV into inclusions, and possibly prevents EV formation. Here, we provide evidence that A26 forms a disulfide-bonded complex with A27 that is anchored to the MV through a noncovalent interaction with the A17 transmembrane protein. In the absence of A27, A26 was unstable, and only small amounts were detected. The interaction of A26 with A27 depended on a C-terminal segment of A26 with 45% amino acid identity to A27. Deletion of A26 failed to enhance EV formation by vaccinia virus, as had been predicted. Nevertheless, the interaction of A26 and A27 may have functional significance, since each is thought to mediate binding to cells through interaction with laminin and heparan sulfate, respectively. We also found that A26 formed a noncovalent complex with A25, a truncated form of the cowpox virus A-type inclusion matrix protein. The latter association suggests a mechanism for incorporation of virions into A-type inclusions in other orthopoxvirus strains.

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