| Full text | |
| Author(s): |
Souza, Bruna B. S.
;
Lourenco, Thiago C.
;
Gerbelli, Barbara B.
;
Oseliero Filho, Pedro L.
;
Oliveira, Cristiano L. P.
;
Miranda, Antonio
;
da Silva, Emerson R.
Total Authors: 7
|
| Document type: | Journal article |
| Source: | JOURNAL OF MOLECULAR LIQUIDS; v. 368, p. 11-pg., 2022-11-11. |
| Abstract | |
The compaction of long DNA strands into confined spaces such as the nuclei of eukaryotic cells is an essential phenomenon towards the emergence of elaborated forms of life. Histones and protamines are the major nucleoproteins involved in this task participating in the formation of chromatin in somatic and germinative cells, respectively. In addition to a fundamental understanding of critical biological processes, DNA condensation also holds strong potential in biotechnology. Herein, we investigate the mesoscale structure of complexes formed between DNA and histones or protamines. A sophisticated set of biophysical methods encompassing steady-state fluorimetry, small-angle X-ray scattering and infrared nano spectroscopy was used to unveil both the self-assembly and molecular interactions of these complexes. We explored the fluorescence of a molecular rotor, thioflavin T, to investigate the accessibility of ligands in the inter-base environment of DNA strands. AFM-based infrared spectroscopy was used for the first time to probe the vibrational signature of individual DNA/nucleoprotein nano assemblies and disclose secondary-structure features. Our results show that protamines form highly compact structures in which DNA folding hinders access to the inter-base spacing. These assemblies exhibit diversified secondary-structure conformations, with the presence of b-sheets stabilizing the packing. In contrast, histone-based complexes are characterized by fibrillar nano assemblies exhibiting larger inter strands separations and access to guest molecules that intercalate between bases. The findings presented here may help the understanding of DNA condensation mediated by these two major nucleoproteins and may assist the optimization of gene vehicles based on these promising nano assemblies. (c) 2022 Elsevier B.V. All rights reserved. (AU) | |
| FAPESP's process: | 20/13204-7 - The role of mesoporous silica morphology in the incorporation of diphtheria and tetanus anatoxins: potential adjuvants for oral vaccines |
| Grantee: | Pedro Leonidas Oseliero Filho |
| Support Opportunities: | Scholarships abroad - Research Internship - Post-doctor |
| FAPESP's process: | 18/05888-3 - Biosensors based on amphiphilic peptides for detection and diagnosis of diseases |
| Grantee: | Barbara Bianca Gerbelli |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 19/12301-1 - Synthesis of ordered mesoporous silica with different structures and morphologies |
| Grantee: | Pedro Leonidas Oseliero Filho |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 20/02192-8 - Structural investigation of lipid and amphiphilic peptides via Langmuir and Langmuir-Blodgett films |
| Grantee: | Barbara Bianca Gerbelli |
| Support Opportunities: | Scholarships abroad - Research Internship - Post-doctor |