Scaling Concepts in Serpin Polymer Physics
<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-Antitrypsin is a protease inhibitor belonging...
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MDPI AG
2021-05-01
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| Online Access: | https://www.mdpi.com/1996-1944/14/10/2577 |
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| author | Samuele Raccosta Fabio Librizzi Alistair M. Jagger Rosina Noto Vincenzo Martorana David A. Lomas James A. Irving Mauro Manno |
| author_facet | Samuele Raccosta Fabio Librizzi Alistair M. Jagger Rosina Noto Vincenzo Martorana David A. Lomas James A. Irving Mauro Manno |
| author_sort | Samuele Raccosta |
| collection | DOAJ |
| description | <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-Antitrypsin is a protease inhibitor belonging to the serpin family. Serpin polymerisation is at the core of a class of genetic conformational diseases called serpinopathies. These polymers are known to be unbranched, flexible, and heterogeneous in size with a beads-on-a-string appearance viewed by negative stain electron microscopy. Here, we use atomic force microscopy and time-lapse dynamic light scattering to measure polymer size and shape for wild-type (M) and Glu342→Lys (Z) <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-antitrypsin, the most common variant that leads to severe pathological deficiency. Our data for small polymers deposited onto mica and in solution reveal a power law relation between the polymer size, namely the end-to-end distance or the hydrodynamic radius, and the polymer mass, proportional to the contour length. We use the scaling concepts of polymer physics to assess that <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-antitrypsin polymers are random linear chains with a low persistence length. |
| first_indexed | 2024-03-10T11:23:19Z |
| format | Article |
| id | doaj.art-cc447ac5a91645829f8fdfeda2859887 |
| institution | Directory Open Access Journal |
| issn | 1996-1944 |
| language | English |
| last_indexed | 2024-03-10T11:23:19Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Materials |
| spelling | doaj.art-cc447ac5a91645829f8fdfeda28598872023-11-21T19:54:14ZengMDPI AGMaterials1996-19442021-05-011410257710.3390/ma14102577Scaling Concepts in Serpin Polymer PhysicsSamuele Raccosta0Fabio Librizzi1Alistair M. Jagger2Rosina Noto3Vincenzo Martorana4David A. Lomas5James A. Irving6Mauro Manno7Institute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, ItalyInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, ItalyUCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UKInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, ItalyInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, ItalyUCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UKUCL Respiratory, University College London, 5 University Street, London WC1E 6JF, UKInstitute of Biophysics, National Research Council of Italy, via Ugo La Malfa 153, 90146 Palermo, Italy<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-Antitrypsin is a protease inhibitor belonging to the serpin family. Serpin polymerisation is at the core of a class of genetic conformational diseases called serpinopathies. These polymers are known to be unbranched, flexible, and heterogeneous in size with a beads-on-a-string appearance viewed by negative stain electron microscopy. Here, we use atomic force microscopy and time-lapse dynamic light scattering to measure polymer size and shape for wild-type (M) and Glu342→Lys (Z) <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-antitrypsin, the most common variant that leads to severe pathological deficiency. Our data for small polymers deposited onto mica and in solution reveal a power law relation between the polymer size, namely the end-to-end distance or the hydrodynamic radius, and the polymer mass, proportional to the contour length. We use the scaling concepts of polymer physics to assess that <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mi>α</mi><mn>1</mn></msub></semantics></math></inline-formula>-antitrypsin polymers are random linear chains with a low persistence length.https://www.mdpi.com/1996-1944/14/10/2577serpinsserpin polymersatomic force microscopydynamic light scatteringconformational diseasepolymer theory |
| spellingShingle | Samuele Raccosta Fabio Librizzi Alistair M. Jagger Rosina Noto Vincenzo Martorana David A. Lomas James A. Irving Mauro Manno Scaling Concepts in Serpin Polymer Physics Materials serpins serpin polymers atomic force microscopy dynamic light scattering conformational disease polymer theory |
| title | Scaling Concepts in Serpin Polymer Physics |
| title_full | Scaling Concepts in Serpin Polymer Physics |
| title_fullStr | Scaling Concepts in Serpin Polymer Physics |
| title_full_unstemmed | Scaling Concepts in Serpin Polymer Physics |
| title_short | Scaling Concepts in Serpin Polymer Physics |
| title_sort | scaling concepts in serpin polymer physics |
| topic | serpins serpin polymers atomic force microscopy dynamic light scattering conformational disease polymer theory |
| url | https://www.mdpi.com/1996-1944/14/10/2577 |
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