An integrative study to unlock the self-assembling and interaction studies of chromium-based metallo-catanionic surfactant mixtures with Cytochrome C

Abstract

Surfactant protein interactions have ever been a topic of discussion for a number of reasons, more importantly to understand folding and unfoalding of protein. Herein in this report we have explored that interactions of cytochrome c (cyt c) which is a heme protein and is not involved in many amyloid-related disorders but is responsible for many biological functions such as electron transport chain with metallocatanionic vesicles prepared from Cr metallosurfactants and sodium dodecyl sulphate (SDS). Very interesting comparative studies have been carried out to evaluate the role of hydrophobhicity of metallosurfactant (single and double chain), metal ion and surface charge on metallocatanionic on interactions with this water-soluble protein. The method of formation of metal-embedded catanionic aggregates involve the development of self-assembled aggregates at various molar ratios of cationic and anionic surfactants. The prepared metallocatanionic aggregates from hexadecyltrimethyl ammonium chromium trichloride (CrC I) and bishexadecyltrimethyl ammonium chromium tetrachloride (CrC II) with sodium dodecyl sulphate (SDS) were characterized using various analytical techniques such as conductivity, Dynamic light scattering (DLS), Field emission scanning electron microscopy (FESEM), High resolution transmission electron microscopy (HRTEM), Zeta potential, and Small angle X-ray scattering (SAXS). The mixture of depicts the formation of spherical or disc like aggregates. Further, the selected aggregates at varied molar ratios are were investigated for their influence on the primary, secondary and ternaryinteraction with the selected protein. SDS page experiments revealed that primary structure of cyt c remains intacted at all the studied concentrations except at higher concentration of double chain metallocataionic vesicle. The influence on the secondary structure of protein is being impacted by both electrostatic and hydrophobic interactions. The studies revealed that the aggregates form a ground state complex with protein without affecting its heme structure. The complex structure has been formed due to the invovlement of both polar and non-polar forces.