Veronika Knyazeva

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In connection with the study of the influence of changes in the structure of insulin on its biological activity, we have obtained previously unknown semisynthetic analogs of bovine insulin -[AIa-B ~5, AIa-B ~] insulin (I) and [Phe-B ~6] insulin (II) -by combining the Achain isolated from natural bovine insulin with the corresponding synthetic analogs of the(More)
Within the framework of investigation of the bioregulators of prolactin secretion, we have synthesized a previously unreported pyroglutamyl peptide (I) representing a structural analog of the natural hypothalamic thyrotropin-releasing hormone (TRH) [1, 2], differing from the natural hormone by a single-site replacement of an L-histidine residue in position(More)
Within the framework of investigations devoted to the peptide stimulation of insulin secretion, we have developed a method of synthesis and obtained a previously unreported peptide sequence representing a structural analog of the 16 – 19 somatoliberin sequence [1, 2]. In solving this task, we have studied three possible approaches. In the first case, we(More)
Preliminary experiments showed that a promising approach to the synthesis of I is offered by a stepwise process in solution using a scheme based on peptide chain growth directed from an amino terminal acid residue toward the carboxy peptide chain end. Based on this scheme, we have developed an effective method for the synthesis of(More)
The preparation of compound (I) was based on combining the natural A-chain of bovine insulin with the synthetic [AIa~]-B chain of bovine insulin [i]. The protected synthetic chain was first demasked by treatment with sodium in liquid ammonia in the presence of sodium amide [2] and was then subjected to oxidative sulfitolysis [3]. This gave the(More)
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