DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy
Studies revolving around mechanisms responsible for the development of amyloid-based diseases lay the foundations for the recognition of molecular targets of future to-be-developed treatments. However, the vast number of peptides and proteins known to be responsible for fibril formation, combined wi...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-12-01
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| Series: | Membranes |
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| Online Access: | https://www.mdpi.com/2077-0375/11/1/13 |
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| author | Przemyslaw Jurczak Kosma Szutkowski Slawomir Lach Stefan Jurga Paulina Czaplewska Aneta Szymanska Igor Zhukov |
| author_facet | Przemyslaw Jurczak Kosma Szutkowski Slawomir Lach Stefan Jurga Paulina Czaplewska Aneta Szymanska Igor Zhukov |
| author_sort | Przemyslaw Jurczak |
| collection | DOAJ |
| description | Studies revolving around mechanisms responsible for the development of amyloid-based diseases lay the foundations for the recognition of molecular targets of future to-be-developed treatments. However, the vast number of peptides and proteins known to be responsible for fibril formation, combined with their complexity and complexity of their interactions with various cellular components, renders this task extremely difficult and time-consuming. One of these proteins, human cystatin C (<i>h</i>CC), is a well-known and studied cysteine-protease inhibitor. While being a monomer in physiological conditions, under the necessary stimulus—usually a mutation, it tends to form fibrils, which later participate in the disease development. This process can potentially be regulated (in several ways) by many cellular components and it is being hypothesized that the cell membrane might play a key role in the oligomerization pathway. Studies involving cell membranes pose several difficulties; therefore, an alternative in the form of membrane mimetics is a very attractive solution. Here, we would like to present the first study on <i>h</i>CC oligomerization under the influence of phospholipid liposomes, acting as a membrane mimetic. The protein–mimetic interactions are studied utilizing circular dichroism, nuclear magnetic resonance, and size exclusion chromatography. |
| first_indexed | 2024-03-10T13:48:57Z |
| format | Article |
| id | doaj.art-f67e9152700b4d55ab4a6ec4620c0d98 |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-10T13:48:57Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-f67e9152700b4d55ab4a6ec4620c0d982023-11-21T02:21:57ZengMDPI AGMembranes2077-03752020-12-011111310.3390/membranes11010013DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR SpectroscopyPrzemyslaw Jurczak0Kosma Szutkowski1Slawomir Lach2Stefan Jurga3Paulina Czaplewska4Aneta Szymanska5Igor Zhukov6Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandNanoBioMedical Centre, Adam Mickiewicz University, Wszechnicy Piastowskiej 3, 61-614 Poznań, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandNanoBioMedical Centre, Adam Mickiewicz University, Wszechnicy Piastowskiej 3, 61-614 Poznań, PolandIntercollegiate Faculty of Biotechnology UG & MUG, University of Gdańsk, Gdańsk, Abrahama 58, 80-307 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Adolfa Pawińskiego 5A, 02-106 Warszawa, PolandStudies revolving around mechanisms responsible for the development of amyloid-based diseases lay the foundations for the recognition of molecular targets of future to-be-developed treatments. However, the vast number of peptides and proteins known to be responsible for fibril formation, combined with their complexity and complexity of their interactions with various cellular components, renders this task extremely difficult and time-consuming. One of these proteins, human cystatin C (<i>h</i>CC), is a well-known and studied cysteine-protease inhibitor. While being a monomer in physiological conditions, under the necessary stimulus—usually a mutation, it tends to form fibrils, which later participate in the disease development. This process can potentially be regulated (in several ways) by many cellular components and it is being hypothesized that the cell membrane might play a key role in the oligomerization pathway. Studies involving cell membranes pose several difficulties; therefore, an alternative in the form of membrane mimetics is a very attractive solution. Here, we would like to present the first study on <i>h</i>CC oligomerization under the influence of phospholipid liposomes, acting as a membrane mimetic. The protein–mimetic interactions are studied utilizing circular dichroism, nuclear magnetic resonance, and size exclusion chromatography.https://www.mdpi.com/2077-0375/11/1/13human cystatin CNMR spectroscopy<sup>15</sup>N relaxationphospholipidDMPCliposome |
| spellingShingle | Przemyslaw Jurczak Kosma Szutkowski Slawomir Lach Stefan Jurga Paulina Czaplewska Aneta Szymanska Igor Zhukov DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy Membranes human cystatin C NMR spectroscopy <sup>15</sup>N relaxation phospholipid DMPC liposome |
| title | DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy |
| title_full | DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy |
| title_fullStr | DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy |
| title_full_unstemmed | DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy |
| title_short | DMPC Phospholipid Bilayer as a Potential Interface for Human Cystatin C Oligomerization: Analysis of Protein-Liposome Interactions Using NMR Spectroscopy |
| title_sort | dmpc phospholipid bilayer as a potential interface for human cystatin c oligomerization analysis of protein liposome interactions using nmr spectroscopy |
| topic | human cystatin C NMR spectroscopy <sup>15</sup>N relaxation phospholipid DMPC liposome |
| url | https://www.mdpi.com/2077-0375/11/1/13 |
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