Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity
The influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermo...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-12-01
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| Series: | Biochemistry and Biophysics Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580820301618 |
| _version_ | 1818392369347690496 |
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| author | Anna P. Ilyina Egor V. Sidorsky Artem V. Tregubov Valeria M. Chekova Pavel A. Elistratov Viktoria P. Yamskova Igor A. Yamskov |
| author_facet | Anna P. Ilyina Egor V. Sidorsky Artem V. Tregubov Valeria M. Chekova Pavel A. Elistratov Viktoria P. Yamskova Igor A. Yamskov |
| author_sort | Anna P. Ilyina |
| collection | DOAJ |
| description | The influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermostability. The point of conformational thermal transition (65 °C) was determined, after which the peptide-protein complex passes into a denatured stable state. It was found that the peptide-protein complex in aqueous solutions forms thermostable nanosized particles. It was shown that the peptide-protein complex isolated from cattle sclera shows the properties of chaperone, an inhibitor of model protein aggregation induced by dithiothreitol. |
| first_indexed | 2024-12-14T05:28:19Z |
| format | Article |
| id | doaj.art-f6e57e32469549cda277703f3152eb61 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-14T05:28:19Z |
| publishDate | 2020-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-f6e57e32469549cda277703f3152eb612022-12-21T23:15:27ZengElsevierBiochemistry and Biophysics Reports2405-58082020-12-0124100851Peptide-protein complex from cattle sclera: Structural aspects and chaperone activityAnna P. Ilyina0Egor V. Sidorsky1Artem V. Tregubov2Valeria M. Chekova3Pavel A. Elistratov4Viktoria P. Yamskova5Igor A. Yamskov6Institute for Bioregulation Problems LLC, Russian Federation, 119991, Leninsky Prospect, 45, Moscow, Russia; Corresponding author.A.N.Nesmeyanov Institute of Organoelement Compounds of Russian Academy of Sciences, Russian Federation, St. Vavilova, 28, 119991, Moscow, RussiaInstitute for Bioregulation Problems LLC, Russian Federation, 119991, Leninsky Prospect, 45, Moscow, RussiaInstitute for Bioregulation Problems LLC, Russian Federation, 119991, Leninsky Prospect, 45, Moscow, RussiaInstitute for Bioregulation Problems LLC, Russian Federation, 119991, Leninsky Prospect, 45, Moscow, RussiaInstitute for Bioregulation Problems LLC, Russian Federation, 119991, Leninsky Prospect, 45, Moscow, RussiaA.N.Nesmeyanov Institute of Organoelement Compounds of Russian Academy of Sciences, Russian Federation, St. Vavilova, 28, 119991, Moscow, RussiaThe influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermostability. The point of conformational thermal transition (65 °C) was determined, after which the peptide-protein complex passes into a denatured stable state. It was found that the peptide-protein complex in aqueous solutions forms thermostable nanosized particles. It was shown that the peptide-protein complex isolated from cattle sclera shows the properties of chaperone, an inhibitor of model protein aggregation induced by dithiothreitol.http://www.sciencedirect.com/science/article/pii/S2405580820301618BioregulatorsSerum albuminLysozymeCD spectroscopyChaperones |
| spellingShingle | Anna P. Ilyina Egor V. Sidorsky Artem V. Tregubov Valeria M. Chekova Pavel A. Elistratov Viktoria P. Yamskova Igor A. Yamskov Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity Biochemistry and Biophysics Reports Bioregulators Serum albumin Lysozyme CD spectroscopy Chaperones |
| title | Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity |
| title_full | Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity |
| title_fullStr | Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity |
| title_full_unstemmed | Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity |
| title_short | Peptide-protein complex from cattle sclera: Structural aspects and chaperone activity |
| title_sort | peptide protein complex from cattle sclera structural aspects and chaperone activity |
| topic | Bioregulators Serum albumin Lysozyme CD spectroscopy Chaperones |
| url | http://www.sciencedirect.com/science/article/pii/S2405580820301618 |
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