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Целью данной работы является исследование нативных белковых комплексов, образуемых белками BASP1 и GAP-43 на плазматической мембране аксонных окончаний мозга. Очень важным представляется вопрос, являются ли данные комплексы гомо- и гетероолигомерами белков BASP1 и GAP-43 с высокой степенью агрегации и содержат ли они другие белки. Для решения этой проблемы в данной работе использовался подход, связанный с анализом сшитых нативных белковых комплексов липидных рафтов, полученных из синаптосом мозга крысы.

Brain acid soluble proteins BASP1 and GAP-43 are examples of crucial regulatory proteins of the nerve terminals. They are localized at the inner layer of the plasma membrane of axon terminals. BASP1 and GAP-43 play a critical role in axon growth cone guidance during neural development, participate in nerve regeneration and in maintaining of the synaptic plasticity of the nervous system in the adult organism. BASP1 and GAP-43 are major components of detergent-resistant microdomains of the presynaptic membrane (lipid rafts). These proteins bind to and sequester PI(4,5)P in the inner layer of the plasma membrane. It is thought that formation of BASP1 and GAP-43 oligomers is required for this process. BASP1 and GAP-43 form oligomers similar to that of amyloid proteins. However, it is not related to any pathology, conversely, it is important for the organism's vital functions. It remains unknown whether oligomers formed by BASP1 and GAP-43 at the presynaptic membrane are homo- or heterooligomers. In this work we have investigated the native protein complexes of the lipid rafts. For this purpose, we have suggested two different approaches: the extraction of native protein complexes formed by BASP1 and GAP-43 from lipid rafts without using immunochemical methods and the immunoprecipitation of the lipid rafts protein complexes cross-linked by dithiobis (succinimidyl propionate) (DSP).