Probing amikacin interaction with albumin: A combined multispectral and molecular docking investigation.

The fate of a drug administered to a living organism depends on the pharmacological and pharmacokinetic behavior of drugs. Biological macromolecules like serum albumins have a crucial role in the design and biological safety assessments of drugs. Amikacin as an example of the most used semi-synthetic aminoglycosides antibiotics, is included in the crucial drug list of the World Health Organization.

Spectroscopic aspects on the interaction of nisin with serum albumin: thermodynamic and kinetic studies.

Introduction: Nisin is a bacteriocin produced by and species and has antimicrobial activity against other bacteria. Nisin omits the need to use chemical preservatives in food due to its biological preserving properties.

Methods: In the present study, we investigated nisin interaction with bovine serum albumin (BSA) using fluorescence spectroscopy and surface plasmon resonance (SPR) analysis to obtain information about the mechanisms of BSA complex formation with nisin.

Probing binding mode between sodium acid pyrophosphate and albumin: multi-spectroscopic and molecular docking analysis.

Sodium acid pyrophosphate (SAPP) food additive is widely used as a preservative, bulking agent, chelating agent, emulsifier and pH regulator. It is also used as an improver of color and water retention capacity in the processing of various types of seafood, canned food, cooked meat and flour products. For the first time, we evaluated the SAPP interaction with bovine serum albumin (BSA) using spectroscopic methods including UV-Vis absorption, fluorescence spectroscopy, and surface plasmon resonance, and docking analysis to understand the mechanisms of complex formation and binding.