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Aim: To assess the feasibility and the outcome of endoscopically assisted repair of zygomatico-maxillary complex orbital fractures in a tertiary care hospital., Materials and Methods: A descriptive study was carried out over a period of 2 years (01. 11. 2014-31. 10. 2016). 0°-4 mm endoscopes were used for intra-operative endoscopic exploration. Regular armamentarium for management of maxillofacial trauma along with standard plating systems was used. Commercially available medical grade titanium meshes were utilised for orbital floor reconstruction., Results: Fifty-seven of hundred and twelve surgically managed zygomatico-maxillary complex fractures required orbital exploration. Twenty-one of these had reconstruction of the orbital floor. Endoscopically assisted exploration was performed in 10 of the 21; trans-nasally in three cases, the Caldwell-Luc approach was used in three cases, and in another three, the existing fracture in the anterior wall of the maxilla was utilised. In addition, an endoscopic trans-nasal-sphenoidal approach was opted for to access the orbital apex to manage fractured bone fragments that were impinging on the optic nerve in one of the patients., Conclusion: Endoscopes serve as the primary tool in minimally invasive procedures. They are yet to evolve as a major role player in the maxillofacial arena. The authors conclude that endoscopes are truly beneficial as an adjunct to existing techniques. They hold much promise for the future., Competing Interests: Conflict of interestThe authors declare that they have no conflict interest., (© The Association of Oral and Maxillofacial Surgeons of India 2019.)

There is a need to understand the thermodynamics of interaction of cationic peptides with DNA to design better peptide based non-viral gene delivery vectors. The main aim of this study was to understand the influence of N-terminal hydrophobicity of cationic amphiphilic peptides on thermodynamics of interaction with plasmid DNA. The model peptides used were TATPTD and TATPTDs modified at the N-terminal with hydrophobic amino acids. The thermodynamic binding data from isothermal titration calorimetry were compared with ethidium bromide analysis and ultrafiltration to correlate the binding parameters with the structural features of the various peptides used. It was observed that peptides having a smaller hydrophobic domain at the N-terminal have good DNA condensing ability compared with the ones with a longer hydrophobic domain. Calorimetry of peptides that reached saturation binding indicated that enthalpy and entropy are favorable for the interaction. Moreover, the interaction of these peptides with DNA appears to be predominantly electrostatic.