eISSN: 2221-6197 DOI: 10.31301/2221-6197

Sunflower seed cyclic trypsin inhibitor SFTI-1: structure, practical applications and possible origin

Year: 2026

Pages: 23-45

Number: Volume 18, issue 1

Type: scientific article

Summary:

Proteases are involved in vital processes occurring in living organisms. Proteinaceous inhibitors participate in the regulation of protease activity. Protease inhibitors (PIs) are an important element of the plant immune system and are of interest to medicine as a means of suppressing unwanted protease activity. Biotechnology methods are used to create forms with specified properties based on natural PIs. A unique cyclic trypsin inhibitor (TI) from the seeds of species of the genus Helianthus L. (sunflower) - SFTI-1 - was found as a result of screening N.I. Vavilov All-Russian Institute of Plant Genetic Resources (VIR) seed collection. It is distinguished by its small size (1513 Da), simple structure and relative ease of modification, extremely high stability, ability to penetrate cell membranes, etc. Hundreds of papers on SFTI-1 have been published worldwide, devoted to the design of its new forms specific to human and microbial proteases involved in pathological processes. SFTI-1 derivatives can also be used to protect plants from pests and diseases. The origin of SFTI-1 remains unclear. SFTI-1 is almost identical in structure to the inhibitory loop of the Bowman-Birk protease inhibitor (BBI) from soybeans, but is closed in a ring. The other parts of the molecule that are characteristic of BBI are absent. SFTI-1 is synthesized in a single polypeptide chain with one of the 2S albumins and is found only in sunflower and representatives of the closest genera. Low-molecular-weight TIs (HV-BBIs) similar to SFTI-1 have been found in the skin of amphibians. The prevailing opinion is that BBI, HV-BBI, and SFTI-1 have convergent independent origins. The only hypothesis about the origin of SFTI-1 so far is that tens of millions of years ago, in the gene for the reserve 2S albumin, between the regions encoding the signal peptide and the small subunit of albumin, an additional sequence arose that encoded a small peptide, which evolved into SFTI-1. According to this hypothesis, a powerful and highly specialized TI was formed in sunflower in a relatively short time due to the transformation of a virtually random nucleotide sequence. The review also considers other possible scenarios for the emergence of SFTI-1. Analysis of databases revealed homology between the DNA sequences encoding SFTI-1, HV-BBI and fragments of the sequences of Kasal family PIs. The latter are widespread in animals, plants, and oomycetes, including parasitic ones, suggesting a link between the genes of these inhibitors and the origin of SFTI-1.

Keywords:

sunflower, protease, 2S albumin, trypsin inhibitor, SFTI-1, Bowman-Birk inhibitor, BBI, Kazal inhibitor.

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