Proteins represent extremely susceptible targets for oxidants. Oxidative modifications of proteins may bring about violation of their structure and functionality. It implies that the structures of proteins are not infallible in terms of their antioxidant defence. The protection mechanisms in preventing oxidative damages for proteins within cells are mainly related to a large variety of antioxidant enzymatic systems. In contrast, plasma proteins are scarcely protected by these systems, so the mechanism that provides their functioning in the conditions of generating reactive oxygen species (ROS) seems to be much more complicated. Oxidation of many proteins was long considered as a random process. However, the highly site-specific oxidation processes was convincingly demonstrated for some proteins, indicating that protein structure could be adapted to oxidation. According to our hypothesis, some of the structural elements present in proteins are capable of scavenging ROS to protect other protein structures against ROS toxicity. Various antioxidant elements (distinct subdomains, domains, regions, and polypeptide chains) may act as ROS interceptors, thus mitigating the ROS action on functionally crucial amino acid residues of proteins. In the review, the oxidative modifications of certain plasma proteins, such as α-macroglobulin, serum human albumin, fibrinogen, and fibrin-stabilising factor, which differ drastically in their spatial structures and functions, are analysed. The arguments that demonstrate the possibility of existing hypothetical antioxidant structures are presented. For the first time, the emphasis is being placed on the programmed mechanism of protein oxidation.

Amphiphilic polymers show a rich variety of self-assembly behavior in aqueous solutions. In experimental studies, statistical copolymer or block copolymer architectures are usually investigated because of their ease of synthesis or their structural analogy to surfactants. A copolymer structure that links the two architectures is an alternating copolymer, which is easily accessible by polycondensation reactions. Using alternating hydrophilic and hydrophobic building blocks with varying lengths allows a systematic variation between statistical and multiblock architectures. We synthesized alternating amphiphilic copolymers as polyesters using hydrophobic dicarboxylic acids (C4–C20) and hydrophilic poly­(ethylene glycol) (PEG) units (EG3–EG1000). Copolymers with long EG units were made accessible with the help of a newly developed esterification process. The solution properties of amphiphilic copolymers feature a lower critical solution temperature (LCST) behavior in water, which can be systematically varied over a wide range from 3 to 83 °C by adjusting the lengths of the C n and EG m units. We find that the transition temperature depends linearly on the hydrophobic unit length C m and logarithmically on the hydrophilic length EG n . In the one-phase region, PEG copolymer coils are more compact compared to the respective PEG homopolymers due to hydrophobic interactions between the hydrophobic units leading to loop formation. For shorter PEG units, the copolymers form micellar structures consisting only of a few copolymer chains. The micellar cores consist of hydrophobic regions containing only a few dicarboxylic acid units embedded in a PEG-rich and water-poor matrix. The cores are surrounded by a diluted corona of PEG chains. Further decreasing the PEG unit length leads to the formation of highly swollen gels consisting of networks of interconnected micelles. These can self-assemble to form highly ordered liquid crystalline cubic phases. The study demonstrates how the structure of alternating amphiphilic copolymers can be systematically varied to adjust the thermal solution properties such as the LCST over a wide range, as well as the self-assembly properties varying between single chains, micelles, gels, and highly ordered lyotropic liquid crystals.

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By using the mass-spectrometry method, the oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains induced by its oxidation have been studied. The αC-region has been proven to be the most vulnerable target for the oxidizer (ozone) as compared with the other structural elements of the Aα chain. The Bβ chain mapping shows that the oxidative sites are localized within all the structural elements of the chain in which the β-nodule exhibits high susceptibility to oxidation. The γ chains are the least vulnerable to the oxidizer action. The results obtained demonstrate convincingly that the self-assembly centers dealing with interactions of knob "A": hole "a" are not involved in oxidative modification. It is concluded that the numerous oxidative sites revealed are mainly responsible for inhibiting lateral aggregation of protofibrils. The part of amino acid residues subjected to oxidation is supposed to carry out the antioxidant function.

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