1. Radiation damage on Langmuir monolayers of the anionic 1.2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt)(DPPG) phospholipid at the air-DNA solution interface
Paulo J Gomes, Amélia M P S Gonçalves da Silva, Paulo A Ribeiro, Osvaldo N Oliveira Jr, Maria Raposo Mater Sci Eng C Mater Biol Appl. 2016 Jan 1;58:576-9. doi: 10.1016/j.msec.2015.09.017. Epub 2015 Sep 7.
The resilience of cells to ultraviolet (UV) irradiation is probably associated with the effects induced in biological molecules such as DNA and in the cell membrane. In this study, we investigated UV damage to the anionic 1.2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DPPG) phospholipid, which is an important component of cell membranes. In films cast from DPPG emulsions, UV irradiation induced cleavage of C-O, C=O and -PO(2-) bonds, while in Langmuir monolayers at the air/water interface representing the cell membrane this irradiation caused the monolayer stability to decrease. When DNA was present in the subphase, however, the effects from UV irradiation were smaller, since the ionic products from degradation of either DPPG or DNA stabilize the intact DPPG molecules. This mechanism may explain why UV irradiation does not cause immediate cell collapse, thus providing time for the cellular machinery to repair elements damaged by UV.
2. Radiation damage on Langmuir monolayers of the anionic 1.2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt)(DPPG) phospholipid at the air-DNA solution interface
Paulo J Gomes, Amélia M P S Gonçalves da Silva, Paulo A Ribeiro, Osvaldo N Oliveira Jr, Maria Raposo Mater Sci Eng C Mater Biol Appl. 2016 Jan 1;58:576-9. doi: 10.1016/j.msec.2015.09.017. Epub 2015 Sep 7.
The resilience of cells to ultraviolet (UV) irradiation is probably associated with the effects induced in biological molecules such as DNA and in the cell membrane. In this study, we investigated UV damage to the anionic 1.2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DPPG) phospholipid, which is an important component of cell membranes. In films cast from DPPG emulsions, UV irradiation induced cleavage of C-O, C=O and -PO(2-) bonds, while in Langmuir monolayers at the air/water interface representing the cell membrane this irradiation caused the monolayer stability to decrease. When DNA was present in the subphase, however, the effects from UV irradiation were smaller, since the ionic products from degradation of either DPPG or DNA stabilize the intact DPPG molecules. This mechanism may explain why UV irradiation does not cause immediate cell collapse, thus providing time for the cellular machinery to repair elements damaged by UV.
3. Interaction of cyclotide Kalata B1 protein with model cellular membranes of varied electrostatics
Ritika Gupta, Jyoti Kumari, Soumya Pati, Shailja Singh, Manasi Mishra, Sajal K Ghosh Int J Biol Macromol. 2021 Nov 30;191:852-860. doi: 10.1016/j.ijbiomac.2021.09.147. Epub 2021 Sep 27.
A uni-molecular layer of lipids at air-water interface mimicking one of the leaflets of the cellular membrane provides a simple model to understand the interaction of any foreign molecules with the membrane. Here, the interactions of protein Kalata B1 (KB1) of cyclotide family with the phospholipids 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DPPG), and 1,2-distearoyl-sn-glycero-3-ethylphosphocholine chloride salt (DSEPC) have been investigated. The addition of KB1 induces a change in pressure of the lipid monolayers. The characteristic time of the change in pressure is found to be dependent on the electrostatic nature of the lipid. Even though the protein is weakly surface active, it is capable of modifying the phase behavior and elastic properties of lipid monolayers with differences in their strength and nature making the layers more floppy. The KB1-lipid interaction has been quantified by calculating the excess Gibb's free energy of interaction and the 1-anilino-8-naphthalenesulfonate (ANS) binding studies. The interaction with zwitterionic DPPC and negatively charged DPPG lipids are found to be thermodynamically favorable whereas the protein shows a weaker response to positively charged DSEPC lipid. Therefore, the long ranged electrostatic is the initial driving force for the KB1 to recognize and subsequently attach to a cellular membrane. Thereafter, the hydrophobic region of the protein may penetrate into the hydrophobic core of the membrane via specific amino acid residues.
