Prospects for the use of macrocyclic photosensitizers for inactivation of SARS-CoV-2: selection of compounds leaders based on the molecular docking data.

The treatment of coronavirus COVID-19, like other viral diseases, is currently underdeveloped. This fact necessitates the search for new drugs and treatment methods that will effectively disrupt the life cycle of the virus. A big problem in the therapy of viral diseases is the ability of viruses to evade the host's immune response.

Theoretical and experimental study of interaction of macroheterocyclic compounds with ORF3a of SARS-CoV-2.

The pandemic infectious disease (Covid-19) caused by the coronavirus (SARS-CoV2) is spreading rapidly around the world. Covid-19 does an irreparable harm to the health and life of people. It also has a negative financial impact on the economies of most countries of the world.

Destruction of Chitosan and Its Complexes with Cobalt(II) and Copper(II) Tetrasulphophthalocyanines.

Chitosan is a naturally occurring polysaccharide derived from chitin with a wide range of uses. Phthalocyanines are macroheterocyclic compounds that have a number of useful properties such as coloring and catalytic and antioxidant activity. Phthalocyanines are able to immobilize on chitosan, forming complexes with new useful properties.

Modeling the binding of protoporphyrin IX, verteporfin, and chlorin e6 to SARS-CoV-2 proteins.

In this work, we analyze the latest data on the molecular docking of a range of SARS-CoV-2 proteins to protoporphyrin IX, verteporfin, and chlorin e6, as well as consider the prospects for using chlorins and porphyrins as agents for photoinactivation of the SARS2 virus.

Molecular mechanisms causing albumin aggregation. The main role of the porphyrins of the blood group.

In this paper was studied the interaction of deutero- and hematoporphyrin with bovine serum albumin, using various methods of physico-chemical analysis. It was established that the localization of porphyrins occurred in the IB subdomain, while hematoporphyrin interacted with the protein in a monomeric form, and deuteroporphyrin - as a J-dimer. Based on spectral studies, the affinity constants of binding albumin with porphyrins were determined, and the affinity of the protein for deuteroporphyrin appeared to be higher than for hematoporphyrin.