Although fluorine in the form of fluoride minerals is the most abundant halogen in the Earth's crust, only 12 naturally occurring organofluorine compounds have so far been found¹, and how these are biosynthesized remains a mystery². Here we describe an enzymatic reaction that occurs in the bacterium Streptomyces cattleya and which catalyses the conversion of fluoride ion and S-adenosylmethionine (SAM) to 5′-fluoro-5′-deoxyfluoroadenosine (5′-FDA). To our knowledge, this is the first fluorinase enzyme to be identified, a discovery that opens up a new biotechnological opportunity for the preparation of organofluorine compounds.

Colloidal gold solutions have been used for centuries in a wide variety of applications including staining glass and in the colouring of ceramics. More recently, gold nanoparticles (GNPs) have been studied extensively due to their interesting size-dependent electronic and optical properties. GNPs can be functionalized easily with biomolecules that contain thiols, amines, or even phosphine moieties. For example, the reaction of thiol-containing peptides with GNPs has been used extensively to prepare novel hybrid materials for biomedical applications. A range of different types of peptides can be used to access biomaterials that are designed to perform a specific role such as cancer cell targeting. In addition, specific peptide sequences that are responsive to external stimuli (e.g. temperature or pH) can be used to stabilise/destabilise the aggregation of colloidal GNPs. Such systems have exciting potential applications in the field of colorimetric sensing (including bio-sensing) and in targeted drug delivery platforms. In this review, we will give an overview of the current methods used for preparing peptide functionalized GNPs, and we will discuss their key properties outlining the various applications of this class of biomaterial. In particular, the potential applications of peptide functionalized GNPs in areas of sensing and targeted drug delivery will be discussed.

We previously reviewed the use of ¹⁹F NMR in the broad field of chemical biology [Cobb, S. L.; Murphy, C. D. J. Fluorine Chem. 2009, 130, 132–140] and present here a summary of the literature from the last decade that has the technique as the central method of analysis. The topics covered include the synthesis of new fluorinated probes and their incorporation into macromolecules, the application of ¹⁹F NMR to monitor protein–protein interactions, protein–ligand interactions, physiologically relevant ions and in the structural analysis of proteins and nucleic acids. The continued relevance of the technique to investigate biosynthesis and biodegradation of fluorinated organic compounds is also described.

Over the past two decades, developing medical applications for peptides has, and continues to be a highly active area of research. At present there are over 60 peptide‐based drugs on the market and more than 140 in various stages of clinical trials. The interest in peptide‐based therapeutics arises from their biocompatibility and their ability to form defined secondary and tertiary structures, resulting in a high selectivity for complex targets. However, there are significant challenges associated with the development of peptide‐based therapeutics, namely peptides are readily metabolised in vivo. Peptoids are an emerging class of peptidomimetic and they offer an alternative to peptides. Peptoids are comprised of N‐substituted glycines where side‐chains are located on the nitrogen atom of the amide backbone rather than the α‐carbon as is the case in peptides. This change in structure confers a high degree of resistance to proteolytic degradation but the absence of any backbone hydrogen bonding means that peptoids exhibit a high degree of conformational flexibility. Cyclisation has been explored as one possible route to rigidify peptoid structures, making them more selective, and, therefore more desirable as potential therapeutics. This review outlines the various strategies that have been developed over the last decade to access new types of macrocyclic peptoids.