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The data of heterologous expression protocol for synthesis of 15N, 13C-labeled SEM1(68-107) peptide fragment of homo sapiens semenogelin 1.

ABSTRACT: The semenogelin 1 protein is secreted in the seminal vesicles. After ejaculation it is split into small peptide fragments using internal proteases. It was shown that the fragments SEM1(45-107), SEM1(49-107), SEM1(68-107) (SEM1(86-107) form amyloid fibrils, which increase the possibility of HIV infection. The article presents a protocol for the synthesis and purification of a 15N, 13C-labeled SEM1(68-107) peptide for further structural studies by high-resolution NMR spectroscopy. The work describes cloning, expression of fusion protein GB1-SEM1(68-107) in E.coli, its purification, removal of GB1 and purification of SEM1(68-107). The purity of SEM1(68-107) samples on each purification steps was evaluated by polyacrylamide gel electrophoresis under denaturing conditions (SDS-PAGE) and tricine-SDS-PAGE. The developed protocol allows to obtain SEM1(68-107) peptide for NMR studies (using 3D experiments), instead of costly solid-phase synthesis.

SUBMITTER: Bikmullin A 

PROVIDER: S-EPMC8563649 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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The data of heterologous expression protocol for synthesis of <sup>15</sup>N, <sup>13</sup>C-labeled SEM1(68-107) peptide fragment of homo sapiens semenogelin 1.

Bikmullin Aydar A   Klochkova Evelina E   Krasnovid Filipp F   Blokhin Dmitriy D  

MethodsX 20210908

The semenogelin 1 protein is secreted in the seminal vesicles. After ejaculation it is split into small peptide fragments using internal proteases. It was shown that the fragments SEM1(45-107), SEM1(49-107), SEM1(68-107) (SEM1(86-107) form amyloid fibrils, which increase the possibility of HIV infection. The article presents a protocol for the synthesis and purification of a <sup>15</sup>N, <sup>13</sup>C-labeled SEM1(68-107) peptide for further structural studies by high-resolution NMR spectros  ...[more]

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